دورية أكاديمية

Species-specificity of the BamA component of the bacterial outer membrane protein-assembly machinery.

التفاصيل البيبلوغرافية
العنوان: Species-specificity of the BamA component of the bacterial outer membrane protein-assembly machinery.
المؤلفون: Elena B Volokhina, Jan Grijpstra, Frank Beckers, Erika Lindh, Viviane Robert, Jan Tommassen, Martine P Bos
المصدر: PLoS ONE, Vol 8, Iss 12, p e85799 (2013)
بيانات النشر: Public Library of Science (PLoS), 2013.
سنة النشر: 2013
المجموعة: LCC:Medicine
LCC:Science
مصطلحات موضوعية: Medicine, Science
الوصف: The BamA protein is the key component of the Bam complex, the assembly machinery for outer membrane proteins (OMP) in gram-negative bacteria. We previously demonstrated that BamA recognizes its OMP substrates in a species-specific manner in vitro. In this work, we further studied species specificity in vivo by testing the functioning of BamA homologs of the proteobacteria Neisseria meningitidis, Neisseria gonorrhoeae, Bordetella pertussis, Burkholderia mallei, and Escherichia coli in E. coli and in N. meningitidis. We found that no BamA functioned in another species than the authentic one, except for N. gonorrhoeae BamA, which fully complemented a N. meningitidis bamA mutant. E. coli BamA was not assembled into the N. meningitidis outer membrane. In contrast, the N. meningitidis BamA protein was assembled into the outer membrane of E. coli to a significant extent and also associated with BamD, an essential accessory lipoprotein of the Bam complex.Various chimeras comprising swapped N-terminal periplasmic and C-terminal membrane-embedded domains of N. meningitidis and E. coli BamA proteins were also not functional in either host, although some of them were inserted in the OM suggesting that the two domains of BamA need to be compatible in order to function. Furthermore, conformational analysis of chimeric proteins provided evidence for a 16-stranded β-barrel conformation of the membrane-embedded domain of BamA.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 1932-6203
Relation: http://europepmc.org/articles/PMC3869937?pdf=render; https://doaj.org/toc/1932-6203
DOI: 10.1371/journal.pone.0085799
URL الوصول: https://doaj.org/article/66e90b2e9f89457ebf57f7921dca3f54
رقم الأكسشن: edsdoj.66e90b2e9f89457ebf57f7921dca3f54
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:19326203
DOI:10.1371/journal.pone.0085799