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DOI | 10.1073/pnas.2101349118 |
Periscope Proteins are variable-length regulators of bacterial cell surface interactions | |
Whelan F.; Lafita A.; Gilburt J.; Dégut C.; Griffiths S.C.; Jenkins H.T.; St John A.N.; Paci E.; Moir J.W.B.; Plevin M.J.; Baumann C.G.; Bateman A.; Potts J.R. | |
发表日期 | 2021 |
ISSN | 0027-8424 |
卷号 | 118期号:23 |
英文摘要 | Changes at the cell surface enable bacteria to survive in dynamic environments, such as diverse niches of the human host. Here, we reveal “Periscope Proteins” as a widespread mechanism of bacterial surface alteration mediated through protein length variation. Tandem arrays of highly similar folded domains can form an elongated rod-like structure; thus, variation in the number of domains determines how far an N-terminal host ligand binding domain projects from the cell surface. Supported by newly available long-read genome sequencing data, we propose that this class could contain over 50 distinct proteins, including those implicated in host colonization and biofilm formation by human pathogens. In large multidomain proteins, sequence divergence between adjacent domains appears to reduce interdomain misfolding. Periscope Proteins break this “rule,” suggesting that their length variability plays an important role in regulating bacterial interactions with host surfaces, other bacteria, and the immune system. © This open access article is distributed under Creative Commons Attribution License 4.0 (CC BY). |
英文关键词 | Bacterial surface proteins; Multidomain proteins; Protein structure |
语种 | 英语 |
scopus关键词 | article; bacterial cell; biofilm; cell surface; human; immune system; ligand binding; protein domain |
来源期刊 | Proceedings of the National Academy of Sciences of the United States of America |
文献类型 | 期刊论文 |
条目标识符 | http://gcip.llas.ac.cn/handle/2XKMVOVA/238898 |
作者单位 | Department of Biology, The University of York, York, YO10 5DD, United Kingdom; European Molecular Biology Laboratory, European Bioinformatics Institute, Wellcome Genome CampusCB10 1SD, United Kingdom; Department of Chemistry, The University of York, York, YO10 5DD, United Kingdom; Astbury Centre for Structural Molecular Biology, The University of Leeds, Leeds, LS2 9JT, United Kingdom; Department of Molecular and Biomedical Science, The University of Adelaide, Adelaide, SA 5005, Australia; School of Life and Environmental Sciences, University of Sydney, Camperdown, NSW 2006, Australia |
推荐引用方式 GB/T 7714 | Whelan F.,Lafita A.,Gilburt J.,et al. Periscope Proteins are variable-length regulators of bacterial cell surface interactions[J],2021,118(23). |
APA | Whelan F..,Lafita A..,Gilburt J..,Dégut C..,Griffiths S.C..,...&Potts J.R..(2021).Periscope Proteins are variable-length regulators of bacterial cell surface interactions.Proceedings of the National Academy of Sciences of the United States of America,118(23). |
MLA | Whelan F.,et al."Periscope Proteins are variable-length regulators of bacterial cell surface interactions".Proceedings of the National Academy of Sciences of the United States of America 118.23(2021). |
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