2014
DOI: 10.7554/elife.03035
|View full text |Cite
|
Sign up to set email alerts
|

A structural model of the active ribosome-bound membrane protein insertase YidC

Abstract: The integration of most membrane proteins into the cytoplasmic membrane of bacteria occurs co-translationally. The universally conserved YidC protein mediates this process either individually as a membrane protein insertase, or in concert with the SecY complex. Here, we present a structural model of YidC based on evolutionary co-variation analysis, lipid-versus-protein-exposure and molecular dynamics simulations. The model suggests a distinctive arrangement of the conserved five transmembrane domains and a hel… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1

Citation Types

12
107
0

Year Published

2015
2015
2023
2023

Publication Types

Select...
7
1

Relationship

1
7

Authors

Journals

citations
Cited by 77 publications
(119 citation statements)
references
References 47 publications
12
107
0
Order By: Relevance
“…Although the SecYEG translocon overcomes this difficulty by forming a polypeptide-conducting channel that sequesters a translocating polypeptide from the lipidic environment (15)(16)(17), several lines of evidence (19,20,27), most notably the crystal structure of B. halodurans YidC2 (21), suggest that YidC uses a channel-independent mechanism.…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…Although the SecYEG translocon overcomes this difficulty by forming a polypeptide-conducting channel that sequesters a translocating polypeptide from the lipidic environment (15)(16)(17), several lines of evidence (19,20,27), most notably the crystal structure of B. halodurans YidC2 (21), suggest that YidC uses a channel-independent mechanism.…”
Section: Discussionmentioning
confidence: 99%
“…The pore can also open laterally to the lipid phase of the membrane, allowing release of a TM segment of substrates out of the translocon pore to establish membrane protein integration (15)(16)(17). Although earlier electron microscopic studies of Escherichia coli YidC and Saccharomyces cerevisiae Oxa1 led to a proposal that YidC forms a homodimer, which creates a channel-like structure at the subunit interface (18), more recent evidence suggests that a monomer of YidC interacts with the ribosome that is translating a membrane protein (19,20). The crystal structures of YidC from Bacillus halodurans at a resolution up to 2.4 Å (21) revealed that the five TM segments of YidC form a cavity presumably in the lipid bilayer.…”
mentioning
confidence: 99%
“…The chimeric E. coli YidC with an extended C-terminal tail from Rhodopirellula baltica YidC (YidC-Rb) exhibited enhanced binding of translating ribosome forming primary interaction sites on the ribosomal rRNA helix 59 and the ribosomal protein L24, as shown by the cryo-electron microscopy structure of the YidC-Rb⅐RNC complex (26). Lately, Wickles et al (27) built a structural model of E. coli YidC via the intramolecular co-variation analysis, which appeared in agreement with the experimentally solved structure. The model was applied to interpret the interaction of E. coli YidC with the RNC-F 0 c visualized in cryo-electron microscopy.…”
mentioning
confidence: 99%
“…The model was applied to interpret the interaction of E. coli YidC with the RNC-F 0 c visualized in cryo-electron microscopy. The residues Tyr-370 and Tyr-377 in the C1 loop and Asp-488 in the C2 loop of YidC were suggested to be directly engaged in the ribosome binding at His-59 and the protein Leu-23, respectively (27). Substitution of the residues compromised the vegetative growth of cells; however, the role of cytoplasmic loops in ribosome binding and insertion activity of YidC has not been studied.…”
mentioning
confidence: 99%
“…Accumulating data indicate that this process begins at the ribosome exit site, where many protein biogenesis machineries can interact and gain access to the nascent polypeptide. This includes chaperones (1-5) such as trigger factor (TF) (1,4,6,7), Hsp70, and the nascent polypeptide-associated complex (8)(9)(10)(11)(12)(13); modification enzymes (10,(14)(15)(16) such as N-acetyl transferase, methionine aminopeptidase, and arginyl transferase; protein-targeting and translocation machineries such as signal recognition particle (SRP) (17)(18)(19)(20), SecA (21), the SecYEG (or Sec61p) (22,23) and YidC translocases (24,25), and the ribosome-bound quality control complex (26)(27)(28)(29)(30). Engagement of these factors with nascent polypeptides influences their folding, assembly, localization, processing, and quality control.…”
mentioning
confidence: 99%