RRC ID 84966
著者 Ikeda Y, Miyazaki R, Tsukazaki T, Akiyama Y, Mori H.
タイトル Translation arrest cancellation of VemP, a secretion monitor in Vibrio, is regulated by multiple cis and trans factors, including SecY.
ジャーナル J Biol Chem
Abstract VemP is a secretory protein in the Vibrio species that monitors cellular protein-transport activity through its translation arrest, allowing expression of the downstream secD2-secF2 genes in the same operon, which encode components of the protein translocation machinery. When cellular protein-transport function is fully active, secD2/F2 expression remains repressed as VemP translation arrest is canceled immediately. The VemP arrest cancellation occurs on the SecY/E/G translocon in a late stage in the translocation process and requires both trans factors, SecD/F and PpiD/YfgM, and a cis element, Arg-85 in VemP; however, the detailed molecular mechanism remains elusive. This study aimed to elucidate how VemP passing through SecY specifically monitors SecD/F function. Genetic and biochemical studies showed that SecY is involved in the VemP arrest cancellation and that the arrested VemP is stably associated with a specific site in the protein-conducting pore of SecY. VemP-Bla reporter analyses revealed that a short hydrophobic segment adjacent to Arg-85 plays a critical role in the regulated arrest cancellation with its hydrophobicity correlating with the stability of the VemP arrest. We identified Gln-65 and Pro-67 in VemP as novel elements important for the regulation. We propose a model for the regulation of the VemP arrest cancellation by multiple cis elements and trans factors with different roles.
巻・号 300(10)
ページ 107735
公開日 2024-10-1
DOI 10.1016/j.jbc.2024.107735
PII S0021-9258(24)02236-1
PMID 39233231
PMC PMC11470409
MeSH Bacterial Proteins* / genetics Bacterial Proteins* / metabolism Gene Expression Regulation, Bacterial* Protein Biosynthesis Protein Transport Vibrio / genetics Vibrio / metabolism Vibrio cholerae / genetics Vibrio cholerae / metabolism
IF 4.238
リソース情報
原核生物(大腸菌) ME9012 MC4100