The PrsA lipoprotein is essential for protein secretion in Bacillus subtilis and sets a limit for high‐level secretion

Abstract

Mutations of the prsA gene of Bacillus subtilis have indicated that the gene is involved in protein secretion and it encodes a novel component of the cellular secretion machinery. We now demonstrate that the gene product is a membrane-associated lipoprotein, presumably bound to the outer face of the cytoplasmic membrane. Experiments to inactivate the prsA gene with insertions indicated that it is indispensable for viability. The cellular level of PrsA protein was shown to be decreased in prsA mutants with decreased level of exoproteins, consistent with an essential function in protein secretion. An increased amount of cellular PrsA protein was introduced by increasing the copy number of prsA in B. subtilis. This enhanced, from six- to twofold, the secretion of alpha-amylases and a protease in strains, which expressed high levels of these exoenzymes. This suggests that PrsA protein is the rate-limiting component of the secretion machinery, a finding that is of considerable biotechnological interest.

Maturation of Lipoproteins by Type II Signal Peptidase Is Required for Phagosomal Escape of Listeria monocytogenes

“…monocytogenes Expresses a PrsA-like Protein Processed by Lsp-In B. subtilis, the folding catalyst PrsA is a major lipoprotein that is essential for life (24). The chromosome of L. monocytogenes encodes a putative PrsA-like protein (Lmo2219) sharing 45% identity with PrsA of B. subtilis.…”

“…However, in these non-pathogenic species, the absence of SPase II resulted in cold and heat sensitivity. In B. subtilis, SPase II is not required for the development of genetic competence, sporulation, and spore germination although at least eight known lipoproteins are important for these processes (24). Cells lacking SPase II accumulated lipidmodified precursor and mature-like forms of PrsA.…”

Lipoprotein biogenesis in Gram-positive bacteria: knowing when to hold ‘em, knowing when to fold ‘em

“…Several Gram-positive members of the membrane insertase YidC family [75] are putative lipoproteins and there are numerous peptidyl-prolyl isomerase (PPIase; also termed foldase or maturase) lipoproteins in Gram-positive bacteria including the essential PrsA in B. subtilis [76] and FkbA in Streptomyces anulatus (formerly Streptomyces chrysomallus) [77] that most likely accelerate protein folding …”

The prolipoprotein diacylglyceryl transferase (Lgt) of Enterococcus faecalis contributes to virulence

“…In consequence, they are thought to play an important part in host-bacteria interactions, including adaptive responses to environmental changes, adherence, internalization, colonization, toxin synthesis and escape from the immune system (for reviews, see Hutchings et al, 2009;Kovacs-Simon et al, 2011). Moreover, lipoproteins have been reported to play a role in cell envelope stability (Sutcliffe & Harrington, 2004;Nguyen et al, 2010), in post-translocational folding of exported proteins (Kontinen & Sarvas, 1993;Hermans et al, 2006) and in pheromone production (Clewell et al, 2000). Finally, lipoproteins can have diverse enzymic activities and can initiate proinflammatory responses, activating many types of host cells such as monocytes, macrophages, neutrophils and B cells (Hutchings et al, 2009;Kovacs-Simon et al, 2011).…”