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Structural basis of Sec-independent membrane protein insertion by YidC
Newly synthesized membrane proteins must be accurately inserted into the membrane, folded and assembled for proper functioning. The protein YidC inserts its substrates into the membrane, thereby… Expand
Conformational transition of Sec machinery inferred from bacterial SecYE structures
Over 30% of proteins are secreted across or integrated into membranes. Their newly synthesized forms contain either cleavable signal sequences or non-cleavable membrane anchor sequences, which direct… Expand
Structure and function of a membrane component SecDF that enhances protein export
Protein translocation across the bacterial membrane, mediated by the secretory translocon SecYEG and the SecA ATPase, is enhanced by proton motive force and membrane-integrated SecDF, which… Expand
Different modes of SecY–SecA interactions revealed by site-directed in vivo photo-cross-linking
While the SecA ATPase drives protein translocation across the bacterial cytoplasmic membrane by interacting with the SecYEG translocon, molecular details of SecA–SecY interaction remain poorly… Expand
Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase
- Kaoru Kumazaki, T. Kishimoto, +6 authors O. Nureki
- Biology, Medicine
- Scientific reports
- 3 December 2014
Bacterial YidC, an evolutionally conserved membrane protein, functions as a membrane protein chaperone in cooperation with the Sec translocon and as an independent insertase for membrane proteins. In… Expand
Dynamic Viscoelastic Study on the Gelation of 7S Globulin from Soybeans.
7S globulin was isolated according to a new method from soybeans. Its physicochemical properties were studied by differential scanning calorimetry (DSC) and by dynamic viscoelastic measurements.… Expand
Cold shock induction of RNase R and its role in the maturation of the quality control mediator SsrA/tmRNA
In this paper we show that RNase R is a cold shock protein that is induced seven‐ to eightfold by cold shock and that its expression is tightly regulated by temperature. Transcriptional studies… Expand
Crystal structure of the translocation ATPase SecA from Thermus thermophilus reveals a parallel, head-to-head dimer.
- D. Vassylyev, H. Mori, +4 authors K. Ito
- Medicine, Biology
- Journal of molecular biology
- 1 December 2006
The mechanism of pre-protein export through the bacterial cytoplasmic membrane, in which the SecA ATPase plays a crucial role as an "energy supplier", is poorly understood. In particular, biochemical… Expand
The long alpha-helix of SecA is important for the ATPase coupling of translocation.
SecA contains two ATPase folds (NBF1 and NBF2) and other interaction/regulatory domains, all of which are connected by a long helical scaffold domain (HSD) running along the molecule. Here we… Expand
Lipoprotein Receptors Redundantly Participate in Entry of Hepatitis C Virus
Scavenger receptor class B type 1 (SR-B1) and low-density lipoprotein receptor (LDLR) are known to be involved in entry of hepatitis C virus (HCV), but their precise roles and their interplay are not… Expand