{"title":"鉴定拟南芥中一种新的定位在高尔基的假定糖基转移酶蛋白","authors":"Natalia Rzepecka, Yoko Ito, Kei Yura, Emi Ito, Tomohiro Uemura","doi":"10.5511/plantbiotechnology.23.1214a","DOIUrl":null,"url":null,"abstract":"<p><p>SNAREs play an important role in the process of membrane trafficking. In the present research, we investigated subcellular localization of an uncharacterized <i>Arabidopsis thaliana</i> protein reported to interact with a <i>trans</i>-Golgi network-localized Qa-SNARE, SYNTAXIN OF PLANTS 43. Based on the similarity of its amino acid sequence to metazoan fucosyltransferases, we have named this novel protein AtGTLP (<i>Arabidopsis thaliana</i> <b>G</b>lycosyl<b>T</b>ransferase-<b>L</b>ike <b>P</b>rotein) and predicted that it should be a member of yet uncharacterized family of Arabidopsis fucosyltransferases, as it shows no significant sequence similarity to fucosyltransferases previously identified in Arabidopsis. AtGTLP is a membrane-anchored protein, which exhibits a type II-like topology, with a single transmembrane helix and a globular domain in the C-terminal part of its amino acid sequence. Colocalization data we collected suggest that AtGTLP should localize mainly to Golgi apparatus, especially to certain zones of <i>trans</i>-Golgi. As single <i>atgtlp-/-</i> mutants showed no obvious difference in phenotype (primary root length and fresh mass), AtGTLP and proteins related to AtGTLP with high similarity in amino acid sequences may have redundant functions.</p>","PeriodicalId":1,"journal":{"name":"Accounts of Chemical Research","volume":null,"pages":null},"PeriodicalIF":16.4000,"publicationDate":"2024-03-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11500582/pdf/","citationCount":"0","resultStr":"{\"title\":\"Identification of a novel Golgi-localized putative glycosyltransferase protein in <i>Arabidopsis thaliana</i>.\",\"authors\":\"Natalia Rzepecka, Yoko Ito, Kei Yura, Emi Ito, Tomohiro Uemura\",\"doi\":\"10.5511/plantbiotechnology.23.1214a\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>SNAREs play an important role in the process of membrane trafficking. In the present research, we investigated subcellular localization of an uncharacterized <i>Arabidopsis thaliana</i> protein reported to interact with a <i>trans</i>-Golgi network-localized Qa-SNARE, SYNTAXIN OF PLANTS 43. Based on the similarity of its amino acid sequence to metazoan fucosyltransferases, we have named this novel protein AtGTLP (<i>Arabidopsis thaliana</i> <b>G</b>lycosyl<b>T</b>ransferase-<b>L</b>ike <b>P</b>rotein) and predicted that it should be a member of yet uncharacterized family of Arabidopsis fucosyltransferases, as it shows no significant sequence similarity to fucosyltransferases previously identified in Arabidopsis. AtGTLP is a membrane-anchored protein, which exhibits a type II-like topology, with a single transmembrane helix and a globular domain in the C-terminal part of its amino acid sequence. Colocalization data we collected suggest that AtGTLP should localize mainly to Golgi apparatus, especially to certain zones of <i>trans</i>-Golgi. As single <i>atgtlp-/-</i> mutants showed no obvious difference in phenotype (primary root length and fresh mass), AtGTLP and proteins related to AtGTLP with high similarity in amino acid sequences may have redundant functions.</p>\",\"PeriodicalId\":1,\"journal\":{\"name\":\"Accounts of Chemical Research\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":16.4000,\"publicationDate\":\"2024-03-25\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11500582/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Accounts of Chemical Research\",\"FirstCategoryId\":\"5\",\"ListUrlMain\":\"https://doi.org/10.5511/plantbiotechnology.23.1214a\",\"RegionNum\":1,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"CHEMISTRY, MULTIDISCIPLINARY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Accounts of Chemical Research","FirstCategoryId":"5","ListUrlMain":"https://doi.org/10.5511/plantbiotechnology.23.1214a","RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}
引用次数: 0
摘要
SNARE 在膜贩运过程中发挥着重要作用。在本研究中,我们研究了一种未定性的拟南芥蛋白的亚细胞定位,据报道该蛋白与一种跨高尔基网络定位的 Qa-SNARE(植物的 SYNTAXIN 43)相互作用。根据其氨基酸序列与拟南芥岩藻糖基转移酶的相似性,我们将这种新蛋白命名为拟南芥岩藻糖基转移酶样蛋白(AtGTLP),并预测它应该是拟南芥岩藻糖基转移酶家族中尚未表征的成员,因为它与拟南芥中以前发现的岩藻糖基转移酶没有明显的序列相似性。AtGTLP 是一种膜锚定蛋白,具有类似 II 型的拓扑结构,在其氨基酸序列的 C 端部分有一个跨膜螺旋和一个球状结构域。我们收集到的共定位数据表明,AtGTLP 应主要定位在高尔基体,尤其是跨高尔基体的某些区域。由于单个atgtlp-/-突变体在表型(主根长度和新鲜质量)上没有明显差异,AtGTLP和与AtGTLP氨基酸序列高度相似的相关蛋白可能具有冗余功能。
Identification of a novel Golgi-localized putative glycosyltransferase protein in Arabidopsis thaliana.
SNAREs play an important role in the process of membrane trafficking. In the present research, we investigated subcellular localization of an uncharacterized Arabidopsis thaliana protein reported to interact with a trans-Golgi network-localized Qa-SNARE, SYNTAXIN OF PLANTS 43. Based on the similarity of its amino acid sequence to metazoan fucosyltransferases, we have named this novel protein AtGTLP (Arabidopsis thalianaGlycosylTransferase-Like Protein) and predicted that it should be a member of yet uncharacterized family of Arabidopsis fucosyltransferases, as it shows no significant sequence similarity to fucosyltransferases previously identified in Arabidopsis. AtGTLP is a membrane-anchored protein, which exhibits a type II-like topology, with a single transmembrane helix and a globular domain in the C-terminal part of its amino acid sequence. Colocalization data we collected suggest that AtGTLP should localize mainly to Golgi apparatus, especially to certain zones of trans-Golgi. As single atgtlp-/- mutants showed no obvious difference in phenotype (primary root length and fresh mass), AtGTLP and proteins related to AtGTLP with high similarity in amino acid sequences may have redundant functions.
期刊介绍:
Accounts of Chemical Research presents short, concise and critical articles offering easy-to-read overviews of basic research and applications in all areas of chemistry and biochemistry. These short reviews focus on research from the author’s own laboratory and are designed to teach the reader about a research project. In addition, Accounts of Chemical Research publishes commentaries that give an informed opinion on a current research problem. Special Issues online are devoted to a single topic of unusual activity and significance.
Accounts of Chemical Research replaces the traditional article abstract with an article "Conspectus." These entries synopsize the research affording the reader a closer look at the content and significance of an article. Through this provision of a more detailed description of the article contents, the Conspectus enhances the article's discoverability by search engines and the exposure for the research.