Pub Date : 2024-09-30eCollection Date: 2024-01-01DOI: 10.17912/micropub.biology.001300
Sabrice Guerrier, Michael Patterson, Kaitlin Crofton, Michael Tucker, Shyhiem Walker
Changes in lipid composition at membrane fusion sites in mating Tetrahymena are thought to involve the endoplasmic reticulum (ER), but its localization to these sites has not been observed. Here we show ER distribution during Tetrahymena mating using TtRET1-GFP and GFP-KDEL. We find that both markers localize to perinuclear membranes and tubular structures that connect perinuclear membrane to plasma membrane at fusion sites. Interestingly, both markers disappear from parental macronuclei after emergence of zygotic macronuclei. These similarities in localization of established ER marker, GFP-KDEL, and TtRET1-GFP reveal TtRET1-GFP as a useful new live cell marker for the ER in Tetrahymena.
{"title":"Dynamic Localization of Endoplasmic Reticulum during Tetrahymena Conjugation.","authors":"Sabrice Guerrier, Michael Patterson, Kaitlin Crofton, Michael Tucker, Shyhiem Walker","doi":"10.17912/micropub.biology.001300","DOIUrl":"https://doi.org/10.17912/micropub.biology.001300","url":null,"abstract":"<p><p>Changes in lipid composition at membrane fusion sites in mating Tetrahymena are thought to involve the endoplasmic reticulum (ER), but its localization to these sites has not been observed. Here we show ER distribution during Tetrahymena mating using TtRET1-GFP and GFP-KDEL. We find that both markers localize to perinuclear membranes and tubular structures that connect perinuclear membrane to plasma membrane at fusion sites. Interestingly, both markers disappear from parental macronuclei after emergence of zygotic macronuclei. These similarities in localization of established ER marker, GFP-KDEL, and TtRET1-GFP reveal TtRET1-GFP as a useful new live cell marker for the ER in Tetrahymena.</p>","PeriodicalId":74192,"journal":{"name":"microPublication biology","volume":"2024 ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-09-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11474315/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142482445","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-09-30eCollection Date: 2024-01-01DOI: 10.17912/micropub.biology.001344
Kylie M Jozwik, James P Held, Chloe A Hecht, Maulik R Patel
The mitochondrial ribosome (mitoribosome) translates mitochondrial genome encoded proteins essential for cellular energy production. Given this critical role, defects in the mitoribosome can cause mitochondrial stress and manifest as multisystemic diseases. In a screen for unique activators of the mitochondrial unfolded protein response (UPR mt ) in Caenorhabditis elegans , we recovered a strain harboring a missense mutation in the gene encoding mitochondrial ribosome protein S31 ( MRPS-31 )-a component of the mitoribosome small subunit. Herein, we confirm causality of the mrps-31 allele and characterize its induction of UPR mt and impact on organismal development, providing a valuable model for further study of the mitoribosome.
{"title":"A viable hypomorphic mutation in the mitochondrial ribosome subunit, MRPS-31, exhibits mitochondrial dysfunction in <i>C. elegans</i>.","authors":"Kylie M Jozwik, James P Held, Chloe A Hecht, Maulik R Patel","doi":"10.17912/micropub.biology.001344","DOIUrl":"10.17912/micropub.biology.001344","url":null,"abstract":"<p><p>The mitochondrial ribosome (mitoribosome) translates mitochondrial genome encoded proteins essential for cellular energy production. Given this critical role, defects in the mitoribosome can cause mitochondrial stress and manifest as multisystemic diseases. In a screen for unique activators of the mitochondrial unfolded protein response (UPR <sup>mt</sup> ) in <i>Caenorhabditis elegans</i> , we recovered a strain harboring a missense mutation in the gene encoding mitochondrial ribosome protein S31 ( MRPS-31 )-a component of the mitoribosome small subunit. Herein, we confirm causality of the <i>mrps-31</i> allele and characterize its induction of UPR <sup>mt</sup> and impact on organismal development, providing a valuable model for further study of the mitoribosome.</p>","PeriodicalId":74192,"journal":{"name":"microPublication biology","volume":"2024 ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-09-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11474418/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142482444","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-09-30eCollection Date: 2024-01-01DOI: 10.17912/micropub.biology.001163
David Cully, Natalie R Cohen, Peter C Breen, Martin A Newman, Robert H Dowen
The serine/threonine protein kinase SGK-1 is a downstream target of mTOR complex 2 (mTORC2) and is a conserved regulator of growth and metabolism. In C. elegans , mutations in rict-1 , which encodes an essential component of mTORC2, impairs lipid homeostasis and growth; however, these defects are partially suppressed by an activating mutation in SGK-1 , E116K. Here, we describe a stronger gain-of-function mutation in sgk-1 , L112F, that was identified in a forward genetic screen for rict-1 suppressor mutations . This allele will be useful in further dissecting the mTORC2 pathway and provides new insight into the role of this conserved residue in regulating SGK-1 kinase activity.
{"title":"A novel gain-of-function mutation in <i>sgk-1</i> partially suppresses mTORC2 defects.","authors":"David Cully, Natalie R Cohen, Peter C Breen, Martin A Newman, Robert H Dowen","doi":"10.17912/micropub.biology.001163","DOIUrl":"https://doi.org/10.17912/micropub.biology.001163","url":null,"abstract":"<p><p>The serine/threonine protein kinase SGK-1 is a downstream target of mTOR complex 2 (mTORC2) and is a conserved regulator of growth and metabolism. In <i>C. elegans</i> , mutations in <i>rict-1</i> , which encodes an essential component of mTORC2, impairs lipid homeostasis and growth; however, these defects are partially suppressed by an activating mutation in SGK-1 , E116K. Here, we describe a stronger gain-of-function mutation in <i>sgk-1</i> , L112F, that was identified in a forward genetic screen for <i>rict-1</i> suppressor mutations <i>.</i> This allele will be useful in further dissecting the mTORC2 pathway and provides new insight into the role of this conserved residue in regulating SGK-1 kinase activity.</p>","PeriodicalId":74192,"journal":{"name":"microPublication biology","volume":"2024 ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-09-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11474317/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142482443","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-09-26eCollection Date: 2024-01-01DOI: 10.17912/micropub.biology.001290
Hanadi Chammout, Delia L Adkins, Aleece K Al-Olimat, Zeinab Alsaad, Beatrice M Altopp, Tuqa Amer, Feyi O Apampa, Gwendolyn R Avery, Isaac I Bazzi, Emilia D Beck, Elise L Beier, B Shafer Belisle, Lane Benton, Madison M Bolyard, Olivia E Brain, Eldon T Buckner, Shria Roy Chowdhury, Jennifer R Cifranic, Liam Cleary, Tyler R Clum, Autumn M Cruz, Meghan V DeGray, Isabel L Echeverry, Haya El Dana, Sarah K Elkadri, Paige L Estep, Luke R Falke, Hannah J Foor, Anika S Gullapalli, Sandro S Hakim, Hussein B Hazime, Lauren E Heininger, Emma G Hoeft, Lauren M James, Yeowon Jeon, Megan R Johnson, Laine P Jordan, Zayd Khan, Sydney K Kochensparger, Fadi J Koria, Ruby M Krasnow, Veronica Lilly, Eileen Lim, Ian T MacCormack, Andriy Malesh, Mikayla G Mariano, Audrey C Mentzer, Katelyn H Messner, Katlyn C Myers, Emily R Newman, Annie M Richters, Liliana Romero, Adam Rotem, Reese J Saho, Kaname Sawaki, Ashley N Selders, Elizabeth Shockney, Farah A Sobh, Isabelle F Speiser, Breanna M Sproul, Veronica J Sroufe, Antonia Tollkuci, Cassandra C Trevino, Megan A Vapenik, Erin M Wagner, Kayla L Bieser, Jamie L Siders, Justin R Thackeray, Jacob D Kagey
Genetic screens in Drosophila melanogaster have long been used to identify genes found in a variety of developmental, cellular, and behavioral processes. Here we describe the characterization and mapping of a mutation identified in a conditional screen for genetic regulators of cell growth and cell division. Within a Flp/FRT system, mutant G.3.2 results in a reduction of mutant tissue and a rough eye phenotype. We find that G.3.2 maps to the gene cnk , providing further support that cnk is a critical gene in Drosophila eye development. This mutant was characterized, mapped and sequenced by undergraduate students within the Fly-CURE consortium.
{"title":"<i>G.3.2</i> is a novel allele of the gene <i>connector enhancer of ksr</i> ( <i>cnk</i> ) in <i>Drosophila melanogaster</i>.","authors":"Hanadi Chammout, Delia L Adkins, Aleece K Al-Olimat, Zeinab Alsaad, Beatrice M Altopp, Tuqa Amer, Feyi O Apampa, Gwendolyn R Avery, Isaac I Bazzi, Emilia D Beck, Elise L Beier, B Shafer Belisle, Lane Benton, Madison M Bolyard, Olivia E Brain, Eldon T Buckner, Shria Roy Chowdhury, Jennifer R Cifranic, Liam Cleary, Tyler R Clum, Autumn M Cruz, Meghan V DeGray, Isabel L Echeverry, Haya El Dana, Sarah K Elkadri, Paige L Estep, Luke R Falke, Hannah J Foor, Anika S Gullapalli, Sandro S Hakim, Hussein B Hazime, Lauren E Heininger, Emma G Hoeft, Lauren M James, Yeowon Jeon, Megan R Johnson, Laine P Jordan, Zayd Khan, Sydney K Kochensparger, Fadi J Koria, Ruby M Krasnow, Veronica Lilly, Eileen Lim, Ian T MacCormack, Andriy Malesh, Mikayla G Mariano, Audrey C Mentzer, Katelyn H Messner, Katlyn C Myers, Emily R Newman, Annie M Richters, Liliana Romero, Adam Rotem, Reese J Saho, Kaname Sawaki, Ashley N Selders, Elizabeth Shockney, Farah A Sobh, Isabelle F Speiser, Breanna M Sproul, Veronica J Sroufe, Antonia Tollkuci, Cassandra C Trevino, Megan A Vapenik, Erin M Wagner, Kayla L Bieser, Jamie L Siders, Justin R Thackeray, Jacob D Kagey","doi":"10.17912/micropub.biology.001290","DOIUrl":"https://doi.org/10.17912/micropub.biology.001290","url":null,"abstract":"<p><p>Genetic screens in <i>Drosophila melanogaster</i> have long been used to identify genes found in a variety of developmental, cellular, and behavioral processes. Here we describe the characterization and mapping of a mutation identified in a conditional screen for genetic regulators of cell growth and cell division. Within a Flp/FRT system, mutant <i>G.3.2</i> results in a reduction of mutant tissue and a rough eye phenotype. We find that <i>G.3.2</i> maps to the gene <i>cnk</i> , providing further support that <i>cnk</i> is a critical gene in <i>Drosophila</i> eye development. This mutant was characterized, mapped and sequenced by undergraduate students within the Fly-CURE consortium.</p>","PeriodicalId":74192,"journal":{"name":"microPublication biology","volume":"2024 ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-09-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11467748/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142482442","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-09-25eCollection Date: 2024-01-01DOI: 10.17912/micropub.biology.001303
Anne E Backlund, Melanie A Higgins
Sulfoquinovosyldiacylglycerol (SQDG) is a plant sulfolipid that plays a major role in the global sulfur cycle. Bacteria contain sulfoglycolytic pathways that are responsible for metabolizing SQDG which requires initial delipidation by a sulfolipase and sulfoquinovosidase (SQase). Recently, a new group of SQases was discovered and have been categorized in a separate glycoside hydrolase family (GH188). Here we have identified a subset of GH188s with an altered sulfonate binding residue. We found that these GH188s have a distinct dimer interface and are found in unique gene clusters that may represent new sulfoglycolytic pathways. Further investigation into these enzymes could broaden our understanding of this new glycoside hydrolase family and uncover diverse sulfoglycolytic pathways.
{"title":"Identification and analysis of a unique group of glycoside hydrolase family 188 sequences with an altered sulfonate binding residue.","authors":"Anne E Backlund, Melanie A Higgins","doi":"10.17912/micropub.biology.001303","DOIUrl":"10.17912/micropub.biology.001303","url":null,"abstract":"<p><p>Sulfoquinovosyldiacylglycerol (SQDG) is a plant sulfolipid that plays a major role in the global sulfur cycle. Bacteria contain sulfoglycolytic pathways that are responsible for metabolizing SQDG which requires initial delipidation by a sulfolipase and sulfoquinovosidase (SQase). Recently, a new group of SQases was discovered and have been categorized in a separate glycoside hydrolase family (GH188). Here we have identified a subset of GH188s with an altered sulfonate binding residue. We found that these GH188s have a distinct dimer interface and are found in unique gene clusters that may represent new sulfoglycolytic pathways. Further investigation into these enzymes could broaden our understanding of this new glycoside hydrolase family and uncover diverse sulfoglycolytic pathways.</p>","PeriodicalId":74192,"journal":{"name":"microPublication biology","volume":"2024 ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-09-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11465081/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142402273","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-09-25eCollection Date: 2024-01-01DOI: 10.17912/micropub.biology.001329
Nicholas D Serra, Meera V Sundaram
C. elegans nematodes possess expanded families of Hedgehog related (Hh-r) and Patched/Dispatched-related (PTR) proteins but their functional relationship remains unclear. Here we investigated whether CHE-14 , the closest C. elegans ortholog for the Hedgehog transporter Dispatched, was necessary for the secretion of two tagged Hh-r proteins: WRT-10 and GRL-2 . We report that CHE-14 is dispensable for the apical localization of GRL-2 and WRT-10 . We also show that animals lacking CHE-14 and another redundant PTR protein DAF-6 also secrete WRT-10 , suggesting neither are required for secretion of these specific Hh-r proteins.
{"title":"The <i>Caenorhabditis elegans</i> Dispatched ortholog, CHE-14, is dispensable for apical secretion of the Hedgehog-related proteins GRL-2 and WRT-10.","authors":"Nicholas D Serra, Meera V Sundaram","doi":"10.17912/micropub.biology.001329","DOIUrl":"10.17912/micropub.biology.001329","url":null,"abstract":"<p><p><i>C. elegans</i> nematodes possess expanded families of Hedgehog related (Hh-r) and Patched/Dispatched-related (PTR) proteins but their functional relationship remains unclear. Here we investigated whether CHE-14 , the closest <i>C. elegans</i> ortholog for the Hedgehog transporter Dispatched, was necessary for the secretion of two tagged Hh-r proteins: WRT-10 and GRL-2 . We report that CHE-14 is dispensable for the apical localization of GRL-2 and WRT-10 . We also show that animals lacking CHE-14 and another redundant PTR protein DAF-6 also secrete WRT-10 , suggesting neither are required for secretion of these specific Hh-r proteins.</p>","PeriodicalId":74192,"journal":{"name":"microPublication biology","volume":"2024 ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-09-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11465080/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142402275","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-09-25eCollection Date: 2024-01-01DOI: 10.17912/micropub.biology.001255
Elena Mellado-Ortega, Hongwei Jing, Edward Wilkinson, Maria Lois, Lucia Strader
High-throughput imaging enables rapid collection of large datasets and is used widely in many systems. However, this is not often used in plant-based systems due to issues related to the need to mount tissues and autofluorescence of plant metabolites. We therefore developed methodology enabling high-throughput imaging of Arabidopsis roots. In this system, growth media supplemented with India Ink (to block autofluorescence from cotyledons) is poured directly into multi-well coverglass-bottom plates and seedlings grown such that the roots grow down with the gravity vector and along the coverglass, effectively mounting themselves for imaging. This method enables high-throughput imaging of Arabidopsis roots.
{"title":"Methodology to enable high-throughput imaging of Arabidopsis seedlings on cover glass-bottom multiwell plates.","authors":"Elena Mellado-Ortega, Hongwei Jing, Edward Wilkinson, Maria Lois, Lucia Strader","doi":"10.17912/micropub.biology.001255","DOIUrl":"10.17912/micropub.biology.001255","url":null,"abstract":"<p><p>High-throughput imaging enables rapid collection of large datasets and is used widely in many systems. However, this is not often used in plant-based systems due to issues related to the need to mount tissues and autofluorescence of plant metabolites. We therefore developed methodology enabling high-throughput imaging of Arabidopsis roots. In this system, growth media supplemented with India Ink (to block autofluorescence from cotyledons) is poured directly into multi-well coverglass-bottom plates and seedlings grown such that the roots grow down with the gravity vector and along the coverglass, effectively mounting themselves for imaging. This method enables high-throughput imaging of Arabidopsis roots.</p>","PeriodicalId":74192,"journal":{"name":"microPublication biology","volume":"2024 ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-09-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11465074/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142402274","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-09-24eCollection Date: 2024-01-01DOI: 10.17912/micropub.biology.000986
Megan E Lawson, Marjorie Dela Cruz, D'Andrew L Harrington, Jack A Vincent, Chelsey McKenna, Anya Goodman, Daron Barnard, Chinmay P Rele
Gene model for the ortholog of Phosphatase and tensin homolog ( Pten ) in the D. miranda Apr. 2013 (UC Berkeley DroMir_2.2/DmirGB2) Genome Assembly (GenBank Accession: GCA_000269505.2 ) of Drosophila miranda . This ortholog was characterized as part of a developing dataset to study the evolution of the Insulin/insulin-like growth factor signaling pathway (IIS) across the genus Drosophila using the Genomics Education Partnership gene annotation protocol for Course-based Undergraduate Research Experiences.
{"title":"Gene model for the ortholog of <i>Pten</i> in <i>Drosophila miranda</i>.","authors":"Megan E Lawson, Marjorie Dela Cruz, D'Andrew L Harrington, Jack A Vincent, Chelsey McKenna, Anya Goodman, Daron Barnard, Chinmay P Rele","doi":"10.17912/micropub.biology.000986","DOIUrl":"10.17912/micropub.biology.000986","url":null,"abstract":"<p><p>Gene model for the ortholog of Phosphatase and tensin homolog ( <i>Pten</i> ) in the <i>D. miranda</i> Apr. 2013 (UC Berkeley DroMir_2.2/DmirGB2) Genome Assembly (GenBank Accession: GCA_000269505.2 ) of <i>Drosophila miranda</i> . This ortholog was characterized as part of a developing dataset to study the evolution of the Insulin/insulin-like growth factor signaling pathway (IIS) across the genus <i>Drosophila</i> using the Genomics Education Partnership gene annotation protocol for Course-based Undergraduate Research Experiences.</p>","PeriodicalId":74192,"journal":{"name":"microPublication biology","volume":"2024 ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-09-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11461024/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142395761","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-09-23eCollection Date: 2024-01-01DOI: 10.17912/micropub.biology.001319
Emma Hernandez, Joseph Ross, Laurent Dejean
Hybrid offspring dysfunction in cytoplasmic-nuclear hybrids (cybrids) implies that one parent's mitochondrial genome is incompatible with the nuclear genome of the other parent. In Caenorhabditis briggsae , cybrids exhibit increased mitochondrial reactive oxygen species (ROS). In this study, we measured the specific activity of markers for mitochondrial abundance (citrate synthase) and antioxidant enzyme response (catalase) in four C. briggsae cybrid lines. An increase of catalase expression but not in mitochondrial abundance was found in dysfunctional cybrids. This suggests that organisms might compensate for some genetic incompatibilities by modulating gene expression of key oxidative stress enzymes such as catalase.
细胞质-核杂交种(杂交种)的杂交后代功能障碍意味着亲本之一的线粒体基因组与另一亲本的核基因组不相容。在布氏拟尾线虫(Caenorhabditis briggsae)中,杂交种表现出线粒体活性氧(ROS)的增加。在这项研究中,我们测量了四个 C. briggsae 杂交品系中线粒体丰度(柠檬酸合成酶)和抗氧化酶反应(过氧化氢酶)标记物的特异性活性。在功能失调的杂交种中,过氧化氢酶的表达增加,但线粒体丰度没有增加。这表明生物可能会通过调节过氧化氢酶等关键氧化应激酶的基因表达来补偿某些遗传不相容性。
{"title":"Evidence of compensation for mitochondrial reactive oxygen species increase in <i>Caenorhabditis briggsae</i> cytoplasmic-nuclear hybrids.","authors":"Emma Hernandez, Joseph Ross, Laurent Dejean","doi":"10.17912/micropub.biology.001319","DOIUrl":"https://doi.org/10.17912/micropub.biology.001319","url":null,"abstract":"<p><p>Hybrid offspring dysfunction in cytoplasmic-nuclear hybrids (cybrids) implies that one parent's mitochondrial genome is incompatible with the nuclear genome of the other parent. In <i>Caenorhabditis briggsae</i> , cybrids exhibit increased mitochondrial reactive oxygen species (ROS). In this study, we measured the specific activity of markers for mitochondrial abundance (citrate synthase) and antioxidant enzyme response (catalase) in four <i>C. briggsae</i> cybrid lines. An increase of catalase expression but not in mitochondrial abundance was found in dysfunctional cybrids. This suggests that organisms might compensate for some genetic incompatibilities by modulating gene expression of key oxidative stress enzymes such as catalase.</p>","PeriodicalId":74192,"journal":{"name":"microPublication biology","volume":"2024 ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11459262/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142395760","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-09-23eCollection Date: 2024-01-01DOI: 10.17912/micropub.biology.001323
Rhiannon Champagne, Jose Abril, Anne Gaillard
Calcium signaling plays an integral role in neuronal communication and muscle movement. The junctophilin family of proteins are structural components of calcium channels of the endoplasmic reticulum and are implicated in various neurodegenerative disorders. This study examined the function of jph-1 , a gene coding for a junctophilin protein in Caenorhabditis elegans ( C. elegans ), by downregulating jph-1 gene expression using RNAi through bacterial feeding. Downregulation of jph-1 altered the physical morphology and impaired thrashing locomotion in wild-type C. elegans . These results are consistent with those of others in demonstrating a role for jph-1 in muscle physiology.
{"title":"Knockdown of the <i>jph-1</i> gene produces altered nervous system structure and impaired muscle endurance phenotypes in <i>Caenorhabditis elegans</i>.","authors":"Rhiannon Champagne, Jose Abril, Anne Gaillard","doi":"10.17912/micropub.biology.001323","DOIUrl":"https://doi.org/10.17912/micropub.biology.001323","url":null,"abstract":"<p><p>Calcium signaling plays an integral role in neuronal communication and muscle movement. The junctophilin family of proteins are structural components of calcium channels of the endoplasmic reticulum and are implicated in various neurodegenerative disorders. This study examined the function of <i>jph-1</i> , a gene coding for a junctophilin protein in <i>Caenorhabditis elegans ( C. elegans ),</i> by downregulating <i>jph-1</i> gene expression using RNAi through bacterial feeding. Downregulation of <i>jph-1</i> altered the physical morphology and impaired thrashing locomotion in wild-type <i>C. elegans .</i> These results are consistent with those of others in demonstrating a role for <i>jph-1</i> in muscle physiology.</p>","PeriodicalId":74192,"journal":{"name":"microPublication biology","volume":"2024 ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11459261/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142395764","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}