Tailise De Souza G. Rodrigues, A. Maxwell, D. Mercer, Orla Lappin
{"title":"Antimicrobial resistance: a Biochemical Society position statement","authors":"Tailise De Souza G. Rodrigues, A. Maxwell, D. Mercer, Orla Lappin","doi":"10.1042/bio_2022_148","DOIUrl":"https://doi.org/10.1042/bio_2022_148","url":null,"abstract":"","PeriodicalId":35334,"journal":{"name":"Biochemist","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48301943","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
A total of 90 scientists from a range of disciplines came together in Madrid over 21–23 September 2022, to discuss the vibrant field of plant proteostasis. Topics covered included ubiquitination, autophagy, vesicle trafficking, proteostasis and stress, quality control and organellar proteostatic systems. High points included excellent student and early career researcher talks (with a large dose of Spanish flair!) and inspirational keynotes from Helen Walden (University of Glasgow, UK; Biochemical Society Lecture) and Tim Clausen (Research Institute of Molecular Pathology Vienna, Austria; EMBO Lecture) who showcased how state-of-the-art structural biology has informed ubiquitination mechanisms influencing human disease. No protein complex is too big to tackle!Marion Clavel (Gregor Mendel Institute, Vienna, Austria) won the best talk prize with her presentation on the role of selective autophagy in promoting plant survival during virus infection, and the poster winner was Marissa Y. Annis (Cornell University, Ithaca, USA) on Uvr2 and Uvr3 proteins as novel candidate regulators of chloroplast Clp system activity with a potential role in stress response.Overall, the meeting was notable for the extremely high quality of science and a strong sense of community. The meeting is accompanied by a special issue of Essays in Biochemistry on plant proteostasis.
来自不同学科的90名科学家于2022年9月21日至23日聚集在马德里，讨论植物蛋白酶平衡这一充满活力的领域。主题包括泛素化、自噬、囊泡运输、蛋白酶抑制和应激、质量控制和细胞器蛋白酶抑制系统。亮点包括优秀学生和早期职业研究人员的演讲(带有大量的西班牙风格!)和海伦·瓦尔登(英国格拉斯哥大学;生化学会讲座)和Tim Clausen(奥地利维也纳分子病理学研究所;EMBO讲座)，他展示了最先进的结构生物学如何告知泛素化机制影响人类疾病。没有什么蛋白质复合物大到无法解决!Marion Clavel (Gregor Mendel Institute, Vienna, Austria)以其关于病毒感染时选择性自噬在促进植物存活中的作用的演讲获得最佳演讲奖，而Marissa Y. Annis (Cornell University, Ithaca, USA)则以Uvr2和Uvr3蛋白作为叶绿体Clp系统活性的新候选调节因子，并在胁迫反应中发挥潜在作用获得最佳演讲奖。总的来说，这次会议以极高的科学质量和强烈的社区意识而引人注目。会议还附有《生物化学论文集》关于植物蛋白酶的特刊。
{"title":"Meeting reports","authors":"Marco Trujillo, Vicente Rubio, Freddie Theodoulou","doi":"10.1042/bio_2023_108","DOIUrl":"https://doi.org/10.1042/bio_2023_108","url":null,"abstract":"A total of 90 scientists from a range of disciplines came together in Madrid over 21–23 September 2022, to discuss the vibrant field of plant proteostasis. Topics covered included ubiquitination, autophagy, vesicle trafficking, proteostasis and stress, quality control and organellar proteostatic systems. High points included excellent student and early career researcher talks (with a large dose of Spanish flair!) and inspirational keynotes from Helen Walden (University of Glasgow, UK; Biochemical Society Lecture) and Tim Clausen (Research Institute of Molecular Pathology Vienna, Austria; EMBO Lecture) who showcased how state-of-the-art structural biology has informed ubiquitination mechanisms influencing human disease. No protein complex is too big to tackle!Marion Clavel (Gregor Mendel Institute, Vienna, Austria) won the best talk prize with her presentation on the role of selective autophagy in promoting plant survival during virus infection, and the poster winner was Marissa Y. Annis (Cornell University, Ithaca, USA) on Uvr2 and Uvr3 proteins as novel candidate regulators of chloroplast Clp system activity with a potential role in stress response.Overall, the meeting was notable for the extremely high quality of science and a strong sense of community. The meeting is accompanied by a special issue of Essays in Biochemistry on plant proteostasis.","PeriodicalId":35334,"journal":{"name":"Biochemist","volume":"23 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2023-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136245890","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
The traditional Christmas Bioenergetics meeting was held this year at Imperial College London, UK. Normally an in-person meeting, a rail strike prompted the organizers to switch to a hybrid format. Over 150 registered and, to our pleasant surprise, most people were able to attend in person. The meeting opened with the Biochemical Society Keilin Memorial Lecture 2022 given by Professor Leonid Sazanov from the Institute of Science and Technology in Austria who took us through his pioneering research elucidating the structure and function of respiratory complex I. The talk featured a presentation of a new model in which proton transfer occurs via a ‘domino’ mechanism. The lecture was then followed by 14 interesting and high-quality talks by young researchers covering a broad range of topics in bioenergetics, including new methods to study the origin and evolution of photosynthesis, the use of cryo-EM to study various respiratory complexes, the ATP synthase and photosystem II, as well as the design of de novo bioenergetic proteins, among other advances.The Biochemical Society Prize for Best Talk was awarded to Benjamin Nash, from the University of East Anglia, who presented a fascinating talk on the discovery and initial characterization of a previously unknown type of multi-cytochrome protein involved in bacterial respiration, which resembled the ancient bolas throwing weapon. The Biochemical Society Prize for Best Poster went to Bartosz Witek, from the University of Cambridge, who presented his work as a master’s student on the bio-photoelectrochemical characterization of co-cultures of photosynthetic and heterotrophic bacteria.The conference closed with a lively reception where discussion arising from a great day of science continued for a few more hours. Overall, bioenergetics research in the UK is alive and well.
{"title":"Meeting reports","authors":"Tanai Cardona, Peter Nixon","doi":"10.1042/bio_2023_106","DOIUrl":"https://doi.org/10.1042/bio_2023_106","url":null,"abstract":"The traditional Christmas Bioenergetics meeting was held this year at Imperial College London, UK. Normally an in-person meeting, a rail strike prompted the organizers to switch to a hybrid format. Over 150 registered and, to our pleasant surprise, most people were able to attend in person. The meeting opened with the Biochemical Society Keilin Memorial Lecture 2022 given by Professor Leonid Sazanov from the Institute of Science and Technology in Austria who took us through his pioneering research elucidating the structure and function of respiratory complex I. The talk featured a presentation of a new model in which proton transfer occurs via a ‘domino’ mechanism. The lecture was then followed by 14 interesting and high-quality talks by young researchers covering a broad range of topics in bioenergetics, including new methods to study the origin and evolution of photosynthesis, the use of cryo-EM to study various respiratory complexes, the ATP synthase and photosystem II, as well as the design of de novo bioenergetic proteins, among other advances.The Biochemical Society Prize for Best Talk was awarded to Benjamin Nash, from the University of East Anglia, who presented a fascinating talk on the discovery and initial characterization of a previously unknown type of multi-cytochrome protein involved in bacterial respiration, which resembled the ancient bolas throwing weapon. The Biochemical Society Prize for Best Poster went to Bartosz Witek, from the University of Cambridge, who presented his work as a master’s student on the bio-photoelectrochemical characterization of co-cultures of photosynthetic and heterotrophic bacteria.The conference closed with a lively reception where discussion arising from a great day of science continued for a few more hours. Overall, bioenergetics research in the UK is alive and well.","PeriodicalId":35334,"journal":{"name":"Biochemist","volume":"150 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2023-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136245892","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
From enzymes to hormones, proteins are the most versatile macromolecules that serve a vital function throughout all biological systems. In nature, organisms are restricted to a 20 amino acid repertoire, which in turn limits the chemistry. Nature evolves and adapts but currently does so under a “chemistry-limited” circumstance. This in turn has limited the aspirations of protein designers and engineers that aim to expand the functional and structural properties of proteins into new and exciting realms. One way nature has circumvented this problem is to recruit non-proteinaceous cofactors. Another way is to change one of the most fundamental concepts underlying biology: the genetic code. Pyrrolysine and selenocysteine are the two main genetically encodable proteinogenic “21st” amino acids; stop codons are recruited to encode the incorporation during ribosomal polypeptide synthesis. This ability of nature to go beyond the standard 20 amino acid repertoire inspired researchers to engineer the fundamental elements of ribosomal polypeptide synthesis and allow full genetic encoding of non-natural amino acids. This in turn helped advance synthetic biology and protein engineering in ways that were not possible by using the standard 20 amino acids. To this day, a vast repertoire of non-natural amino acids is available and is continuously expanding with increasing scientific needs.
{"title":"Expanding the genetic code: a non-natural amino acid story","authors":"Athena Zitti, Dafydd Jones","doi":"10.1042/bio_2023_102","DOIUrl":"https://doi.org/10.1042/bio_2023_102","url":null,"abstract":"From enzymes to hormones, proteins are the most versatile macromolecules that serve a vital function throughout all biological systems. In nature, organisms are restricted to a 20 amino acid repertoire, which in turn limits the chemistry. Nature evolves and adapts but currently does so under a “chemistry-limited” circumstance. This in turn has limited the aspirations of protein designers and engineers that aim to expand the functional and structural properties of proteins into new and exciting realms. One way nature has circumvented this problem is to recruit non-proteinaceous cofactors. Another way is to change one of the most fundamental concepts underlying biology: the genetic code. Pyrrolysine and selenocysteine are the two main genetically encodable proteinogenic “21st” amino acids; stop codons are recruited to encode the incorporation during ribosomal polypeptide synthesis. This ability of nature to go beyond the standard 20 amino acid repertoire inspired researchers to engineer the fundamental elements of ribosomal polypeptide synthesis and allow full genetic encoding of non-natural amino acids. This in turn helped advance synthetic biology and protein engineering in ways that were not possible by using the standard 20 amino acids. To this day, a vast repertoire of non-natural amino acids is available and is continuously expanding with increasing scientific needs.","PeriodicalId":35334,"journal":{"name":"Biochemist","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43484533","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
The Colworth Medal is an esteemed annual award for outstanding research by a young biochemist of any nationality who has carried out the majority of their work in the UK or Republic of Ireland. Donated in 1963 by Unilever Research Colworth Laboratory, the award is made to an early-career scientist who is within 10 years of receiving their highest qualification. Interviews with past winners from 1963 to 2013 were previously published throughout 2013. To celebrate the 60th anniversary of the Colworth Medal, interviews with our latest winners will appear in The Biochemist throughout 2023. In this issue, we will hear from Dr M. Madan Babu (2014) and Professor Helen Walden (2015).
{"title":"60 years of the Colworth Medal","authors":"Lucy Ollett","doi":"10.1042/bio_2023_107","DOIUrl":"https://doi.org/10.1042/bio_2023_107","url":null,"abstract":"The Colworth Medal is an esteemed annual award for outstanding research by a young biochemist of any nationality who has carried out the majority of their work in the UK or Republic of Ireland. Donated in 1963 by Unilever Research Colworth Laboratory, the award is made to an early-career scientist who is within 10 years of receiving their highest qualification. Interviews with past winners from 1963 to 2013 were previously published throughout 2013. To celebrate the 60th anniversary of the Colworth Medal, interviews with our latest winners will appear in The Biochemist throughout 2023. In this issue, we will hear from Dr M. Madan Babu (2014) and Professor Helen Walden (2015).","PeriodicalId":35334,"journal":{"name":"Biochemist","volume":"33 2 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2023-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136181177","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
R. Wright, D. F. Neres, Patarasuda Chaisupa, J. Bryant
Humanity is faced with an enormous challenge in the coming decades. The world’s population is rapidly growing and we need to produce enough food, fuel, medicine and goods to support this growth in an environmentally sustainable and restorative way. Plants will inevitably provide many solutions to the problems we face, but we need to build environmentally sustainable, carbon-negative industries as soon as possible. Applying protein engineering to accelerate the development of improved crop varieties that can produce more while using less is a promising approach. Here we provide an introduction to the approaches, tools and philosophy of protein engineering, as well as several examples of problems in plant breeding and engineering that protein engineers are currently working to solve.
{"title":"Protein engineering and plants: the evolution of sustainable agriculture","authors":"R. Wright, D. F. Neres, Patarasuda Chaisupa, J. Bryant","doi":"10.1042/bio_2023_101","DOIUrl":"https://doi.org/10.1042/bio_2023_101","url":null,"abstract":"Humanity is faced with an enormous challenge in the coming decades. The world’s population is rapidly growing and we need to produce enough food, fuel, medicine and goods to support this growth in an environmentally sustainable and restorative way. Plants will inevitably provide many solutions to the problems we face, but we need to build environmentally sustainable, carbon-negative industries as soon as possible. Applying protein engineering to accelerate the development of improved crop varieties that can produce more while using less is a promising approach. Here we provide an introduction to the approaches, tools and philosophy of protein engineering, as well as several examples of problems in plant breeding and engineering that protein engineers are currently working to solve.","PeriodicalId":35334,"journal":{"name":"Biochemist","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-02-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"46251193","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Surface plasmon resonance (SPR) has emerged as a powerful optical detection technique for studying the binding behaviour of immobilized ligands and analytes in solution. The technique makes it possible to measure interactions in real time with high sensitivity. Over the past two decades, SPR has become the gold standard for studying biomolecular interactions in biomedical research and drug discovery. The interactions that can be studied are diverse and include protein–protein, protein–small molecule, protein–nucleic acid, protein–carbohydrate, lipid–protein, hybrid systems of biomolecules and non-biological surfaces. SPR allows researchers to determine which molecules interact, how strongly they bind and inform experiments using mutants, truncations or other variations to probe specificity. This article summarizes the principle and experimental set-up and illustrates the utility of SPR using the example of lipid–protein interactions.
{"title":"A beginner’s guide to surface plasmon resonance","authors":"Balindile B. Motsa, R. Stahelin","doi":"10.1042/bio_2022_139","DOIUrl":"https://doi.org/10.1042/bio_2022_139","url":null,"abstract":"Surface plasmon resonance (SPR) has emerged as a powerful optical detection technique for studying the binding behaviour of immobilized ligands and analytes in solution. The technique makes it possible to measure interactions in real time with high sensitivity. Over the past two decades, SPR has become the gold standard for studying biomolecular interactions in biomedical research and drug discovery. The interactions that can be studied are diverse and include protein–protein, protein–small molecule, protein–nucleic acid, protein–carbohydrate, lipid–protein, hybrid systems of biomolecules and non-biological surfaces. SPR allows researchers to determine which molecules interact, how strongly they bind and inform experiments using mutants, truncations or other variations to probe specificity. This article summarizes the principle and experimental set-up and illustrates the utility of SPR using the example of lipid–protein interactions.","PeriodicalId":35334,"journal":{"name":"Biochemist","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-02-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49351786","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pathogenic bacteria such as Yersinia pestis, causative agent of the plague, have a genetic armoury of proteins they use to defend themselves against the immune system when invading a host. Upon invasion, Y. pestis bacteria deploy a molecular cloaking device, made of a protein called Caf1, which allows them to avoid being eaten by a host’s macrophage cells. Caf1 has several interesting structural properties that allow it to carry out this role, such as its ‘non-stick’, bioinert nature. This provides us with a blank canvas for protein engineering, where we can insert different bioactive signals into the protein structure, allowing us to instruct cells in a defined way, e.g., providing them with attachment sites or behavioural cues. We can also exploit Caf1’s unusual properties to use it as a molecular Lego kit, mixing and matching different bioactive Caf1 modules to make multifunctional biomaterials. We aim to use engineered Caf1 proteins to solve problems in the industrial scale production of cells for technologies such as cell therapy and cultivated meat. For example, by mixing adhesive and growth factor signals in a single material, and displaying multiple copies of each signal at once, we can reduce the number of expensive reagents needed. More generally, Caf1 is an excellent example of how bacterial armaments and defences can be re-engineered and adapted to benefit society, rather than cause disease.
{"title":"How the secrets of the Black Death give us sustainable meat","authors":"Daniel T. Peters, J. Lakey","doi":"10.1042/bio_2023_100","DOIUrl":"https://doi.org/10.1042/bio_2023_100","url":null,"abstract":"Pathogenic bacteria such as Yersinia pestis, causative agent of the plague, have a genetic armoury of proteins they use to defend themselves against the immune system when invading a host. Upon invasion, Y. pestis bacteria deploy a molecular cloaking device, made of a protein called Caf1, which allows them to avoid being eaten by a host’s macrophage cells. Caf1 has several interesting structural properties that allow it to carry out this role, such as its ‘non-stick’, bioinert nature. This provides us with a blank canvas for protein engineering, where we can insert different bioactive signals into the protein structure, allowing us to instruct cells in a defined way, e.g., providing them with attachment sites or behavioural cues. We can also exploit Caf1’s unusual properties to use it as a molecular Lego kit, mixing and matching different bioactive Caf1 modules to make multifunctional biomaterials. We aim to use engineered Caf1 proteins to solve problems in the industrial scale production of cells for technologies such as cell therapy and cultivated meat. For example, by mixing adhesive and growth factor signals in a single material, and displaying multiple copies of each signal at once, we can reduce the number of expensive reagents needed. More generally, Caf1 is an excellent example of how bacterial armaments and defences can be re-engineered and adapted to benefit society, rather than cause disease.","PeriodicalId":35334,"journal":{"name":"Biochemist","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-02-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"46361169","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Gaining experience in genomics to study heavy metal tolerance in bacteria","authors":"C. Crane-Robinson, N. Sapojnikova","doi":"10.1042/bio_2022_126","DOIUrl":"https://doi.org/10.1042/bio_2022_126","url":null,"abstract":"","PeriodicalId":35334,"journal":{"name":"Biochemist","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-01-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49105325","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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