Identification of diverse archaeal proteins with class III signal peptides cleaved by distinct archaeal prepilin peptidases.

ABSTRACT: Most secreted archaeal proteins are targeted to the membrane via a tripartite signal composed of a charged N terminus and a hydrophobic domain, followed by a signal peptidase-processing site. Signal peptides of archaeal flagellins, similar to class III signal peptides of bacterial type IV pilins, are distinct in that their processing sites precede the hydrophobic domain, which is crucial for assembly of these extracytoplasmic structures. To identify the complement of archaeal proteins with class III signal sequences, a PERL program (FlaFind) was written. A diverse set of proteins was identified, and many of these FlaFind positives were encoded by genes that were cotranscribed with homologs of pilus assembly genes. Moreover, structural conservation of primary sequences between many FlaFind

SUBMITTER: Szabo Z 

PROVIDER: S-EPMC1797317 | biostudies-literature | 2007 Feb

REPOSITORIES: biostudies-literature