首页 | 本学科首页   官方微博 | 高级检索  
   检索      


Wide variation in the cyanobacterial complement of presumptive penicillin-binding proteins
Authors:Email author" target="_blank">Francisco?LeganésEmail author  Amaya?Blanco-Rivero  Francisca?Fernández-Pi?as  Miguel?Redondo  Eduardo?Fernández-Valiente  Qing?Fan  Sigal?Lechno-Yossef  C?Peter?Wolk
Institution:Departamento de Biología, Facultad de Ciencias, Universidad Autónoma de Madrid, 28049 Madrid, Spain. francisco.leganes@uam.es
Abstract:A genomic analysis of putative penicillin-binding proteins (PBPs) that are involved in the synthesis of the peptidoglycan layer of the cell wall and are encoded in 12 cyanobacterial genomes was performed in order to help elucidate the role(s) of these proteins in peptidoglycan synthesis, especially during cyanobacterial cellular differentiation. The analysis suggested that the minimum set of PBPs needed to assemble the peptidoglycan layer in cyanobacteria probably does not exceed one bifunctional transpeptidase–transglycosylase Class A high-molecular-weight PBP; two Class B high-molecular-weight PBPs, one of them probably involved in cellular elongation and the other in septum formation; and one low-molecular-weight PBP. The low-molecular-weight PBPs of all of the cyanobacteria analyzed are putative endopeptidases and are encoded by fewer genes than in Escherichia coli. We show that in Anabaena sp. strain PCC 7120, predicted proteins All2981 and Alr4579, like Alr5101, are Class A high-molecular-weight PBPs that are required for the functional differentiation of aerobically diazotrophic heterocysts, indicating that some members of this class of PBPs are required specifically for cellular developmental processes.
Keywords:Cyanobacteria  Cell differentiation  Cell shape  Fox genes  Penicillin-binding protein  Peptidoglycan  Heterocysts
本文献已被 PubMed SpringerLink 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号