scholarly journals Biotinylation in vivo as a sensitive indicator of protein secretion and membrane protein insertion.

1996 ◽  
Vol 178 (11) ◽  
pp. 3049-3058 ◽  
Author(s):  
G Jander ◽  
J E Cronan ◽  
J Beckwith
Keyword(s):  
Membrane Protein ◽  
Protein Secretion ◽  
Sensitive Indicator ◽  
Protein Insertion ◽  
Membrane Protein Insertion

scholarly journals SRP19 Is a Dispensable Component of the Signal Recognition Particle in Archaea

2006 ◽  
Vol 189 (1) ◽  
pp. 276-279 ◽  
Author(s):  
Sophie Yurist ◽  
Idit Dahan ◽  
Jerry Eichler
Keyword(s):  
Cell Growth ◽  
Membrane Protein ◽  
Protein Secretion ◽  
Signal Recognition Particle ◽  
Haloferax Volcanii ◽  
Signal Recognition ◽  
Protein Insertion ◽  
Membrane Protein Insertion ◽  
Srp Rna

ABSTRACT In vitro, archaeal SRP54 binds SRP RNA in the absence of SRP19, suggesting the latter to be expendable in Archaea. Accordingly, the Haloferax volcanii SRP19 gene was deleted. Although normally transcribed at a level comparable to that of the essential SRP54 gene, SRP19 deletion had no effect on cell growth, membrane protein insertion, protein secretion, or ribosome levels. The absence of SRP19 did, however, increase membrane bacterioruberin levels.

scholarly journals Subunit cooperation in the Get1/2 receptor promotes tail-anchored membrane protein insertion

2021 ◽  
Vol 220 (11) ◽  
Author(s):  
Un Seng Chio ◽  
Yumeng Liu ◽  
SangYoon Chung ◽  
Woo Jun Shim ◽  
Sowmya Chandrasekar ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Eukaryotic Cells ◽  
Protein Insertion ◽  
Protein Biogenesis ◽  
Cytosolic Domains ◽  
Membrane Protein Insertion ◽  
The Individual ◽  
Molecular Recognition Features

The guided entry of tail-anchored protein (GET) pathway, in which the Get3 ATPase delivers an essential class of tail-anchored membrane proteins (TAs) to the Get1/2 receptor at the endoplasmic reticulum, provides a conserved mechanism for TA biogenesis in eukaryotic cells. The membrane-associated events of this pathway remain poorly understood. Here we show that complex assembly between the cytosolic domains (CDs) of Get1 and Get2 strongly enhances the affinity of the individual subunits for Get3•TA, thus enabling efficient capture of the targeting complex. In addition to the known role of Get1CD in remodeling Get3 conformation, two molecular recognition features (MoRFs) in Get2CD induce Get3 opening, and both subunits are required for optimal TA release from Get3. Mutation of the MoRFs attenuates TA insertion into the ER in vivo. Our results demonstrate extensive cooperation between the Get1/2 receptor subunits in the capture and remodeling of the targeting complex, and emphasize the role of MoRFs in receptor function during membrane protein biogenesis.

Structure of YidC from Thermotoga maritima and its implications for YidC‐mediated membrane protein insertion

2018 ◽  
Vol 32 (5) ◽  
pp. 2411-2421 ◽  
Author(s):  
Yanlong Xin ◽  
Yan Zhao ◽  
Jiangge Zheng ◽  
Haizhen Zhou ◽  
Xuejun Cai Zhang ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Thermotoga Maritima ◽  
Protein Insertion ◽  
Membrane Protein Insertion

Membrane protein import in yeast mitochondria

2000 ◽  
Vol 28 (4) ◽  
pp. 495-499 ◽  
Author(s):  
K. Tokatlidis ◽  
S. Vial ◽  
P. Luciano ◽  
M. Vergnolle ◽  
S. Clémence
Keyword(s):  
Membrane Protein ◽  
Molecular Mechanism ◽  
Protein Import ◽  
Mitochondrial Matrix ◽  
Yeast Mitochondria ◽  
Inner Membrane ◽  
Protein Insertion ◽  
The Past ◽  
Membrane Protein Insertion ◽  
Membrane Bound

The protein import pathway that targets proteins to the mitochondrial matrix has been extensively characterized in the past 15 years. Variations of this import pathway account for the sorting of proteins to other compartments as well, but the insertion of integral inner membrane proteins lacking a presequence is mediated by distinct translocation machinery. This consists of a complex of Tim9 and Tim10, two homologous, Zn2+-binding proteins that chaperone the passage of the hydrophobic precursor across the aqueous inter-membrane space. The precursor is then targeted to another, inner-membrane-bound, complex of at least five subunits that facilitates insertion. Biochemical and genetic experiments have identified the key components of this process; we are now starting to understand the molecular mechanism. This review highlights recent advances in this new membrane protein insertion pathway.

Sign in / Sign up

Export Citation Format

Share Document