1999
DOI: 10.1074/jbc.274.35.24585
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Signal Peptide Peptidase- and ClpP-like Proteins of Bacillus subtilis Required for Efficient Translocation and Processing of Secretory Proteins

Abstract: Signal peptides direct the export of secretory proteins from the cytoplasm. After processing by signal peptidase, they are degraded in the membrane and cytoplasm. The resulting fragments can have signaling functions. These observations suggest important roles for signal peptide peptidases. The present studies show that the Gram-positive eubacterium Bacillus subtilis contains two genes for proteins, denoted SppA and TepA, with similarity to the signal peptide peptidase A of Escherichia coli. Notably, TepA also … Show more

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Cited by 73 publications
(94 citation statements)
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“…Because FtsQ has been shown to interact with components of SecYEG translocon (25), it is possible that FtsQ participates in the delivery of Cfp-10 to the SecYEG translocon. Furthermore, we detected a positive interaction between Cfp-10 and the AAA-ATPase chaperone ClpC1 (a member of the Clp͞Hsp100 family of proteins), which are involved in diverse functions, including secretion, gene regulation, protein refolding, and degradation (26,27) and have been shown to associate with the translocation machinery in the chloroplast membrane (28). It may well be that Mtb ClpC1 facilitates Cfp-10 secretion by associating with the translocation complex in the membrane.…”
Section: Discussionmentioning
confidence: 86%
“…Because FtsQ has been shown to interact with components of SecYEG translocon (25), it is possible that FtsQ participates in the delivery of Cfp-10 to the SecYEG translocon. Furthermore, we detected a positive interaction between Cfp-10 and the AAA-ATPase chaperone ClpC1 (a member of the Clp͞Hsp100 family of proteins), which are involved in diverse functions, including secretion, gene regulation, protein refolding, and degradation (26,27) and have been shown to associate with the translocation machinery in the chloroplast membrane (28). It may well be that Mtb ClpC1 facilitates Cfp-10 secretion by associating with the translocation complex in the membrane.…”
Section: Discussionmentioning
confidence: 86%
“…Both, SppA and YqeZ are s W -controlled (Huang et al, 1999;Wiegert et al, 2001), and for YqeZ a function for immunity against sublancin rather than degradation of signal peptides has been shown (Butcher & Helmann, 2006). For SppA (YteI) and TepA (YmfB), a function in degradation of proteins or (signal) peptides that are inhibitory to protein translocation has been proposed (Bolhuis et al, 1999). Signal peptide peptidases described for eukaryotes belong to the group of intramembrane cleaving proteases, and attack certain signal peptides after they have been clipped from newly synthesized secretory or membrane proteins (Weihofen & Martoglio, 2003).…”
Section: Discussionmentioning
confidence: 99%
“…E. coli SppA (protease IV) has been shown to degrade the processed signal sequence of the major lipoprotein, but it is not the only protease that is responsible for signal peptide digestion in the cell envelope (Suzuki et al, 1987). For B. subtilis, three proteins similar to SppA have been described (TepA, SppA and YqeZ; Bolhuis et al, 1999;Helmann, 2002). Both, SppA and YqeZ are s W -controlled (Huang et al, 1999;Wiegert et al, 2001), and for YqeZ a function for immunity against sublancin rather than degradation of signal peptides has been shown (Butcher & Helmann, 2006).…”
Section: Discussionmentioning
confidence: 99%
“…Exceptions include the fosB fosfomycin-resistance gene (Cao et al, 2001), the pbpE penicillin-binding protein (Popham and Setlow, 1993), and sppA which may play a role in degradation of cleaved signal peptides (Bolhuis et al, 1999). Bioinformatic analysis suggests that several other σ W -dependent operons may function in bacteriocin or antibiotic resistance (Cao et al, 2002b).…”
Section: Discussionmentioning
confidence: 99%