scholarly journals In vitro protein translocation into inverted membrane vesicles prepared fromVibrio alginolyticusis stimulated by the electrochemical potential of Na+in the presence ofEscherichia coliSecA

FEBS Letters ◽  
1990 ◽  
Vol 264 (1) ◽  
pp. 10-12 ◽  
Author(s):  
Hajime Tokuda ◽  
Young Jae Kim ◽  
Shoji Mizushima
Keyword(s):  
Protein Translocation ◽  
Membrane Vesicles ◽  
Electrochemical Potential ◽  
Inverted Membrane Vesicles ◽  
Vitro Protein

scholarly journals Substrate Proteins Take Shape at an Improved Bacterial Translocon

2018 ◽  
Vol 201 (1) ◽  
Author(s):  
Donald Oliver
Keyword(s):  
Protein Transport ◽  
Protein Translocation ◽  
Membrane Vesicles ◽  
Transport Models ◽  
Content Type ◽  
Rate Limiting ◽  
Substrate Proteins

ABSTRACTCharacterization of Sec-dependent bacterial protein transport has often relied on anin vitroprotein translocation system comprised in part ofEscherichia coliinverted inner membrane vesicles or, more recently, purified SecYEG translocons reconstituted into liposomes using mostly a single substrate (proOmpA). A paper published in this issue (P. Bariya and L. Randall, J Bacteriol 201:e00493-18, 2019, https://doi.org/10.1128/JB.00493-18) finds that inclusion of SecA protein during SecYEG proteoliposome reconstitution dramatically improves the number of active translocons. This experimentally useful and intriguing result that may arise from SecA membrane integration properties is discussed here. Furthermore, determination of the rate-limiting transport step for nine different substrates implicates the mature region distal to the signal peptide in the observed rate constant differences, indicating that more nuanced transport models that respond to differences in protein sequence and structure are needed.

scholarly journals SecA Dimer Cross-Linked at Its Subunit Interface Is Functional for Protein Translocation

2006 ◽  
Vol 188 (1) ◽  
pp. 335-338 ◽  
Author(s):  
Lucia B. Jilaveanu ◽  
Donald Oliver
Keyword(s):  
Conformational Changes ◽  
Protein Transport ◽  
Protein Translocation ◽  
Directed Mutagenesis ◽  
Subunit Interface ◽  
Cargo Proteins ◽  
Considerable Controversy ◽  
The Subject ◽  
Vitro Protein

ABSTRACT SecA facilitates protein transport across the eubacterial plasma membrane by its association with cargo proteins and the SecYEG translocon, followed by ATP-driven conformational changes that promote protein translocation in a stepwise manner. Whether SecA functions as a monomer or a dimer during this process has been the subject of considerable controversy. Here we utilize cysteine-directed mutagenesis along with the crystal structure of the SecA dimer to create a cross-linked dimer at its subunit interface, which was normally active for in vitro protein translocation.

scholarly journals Sheep pancreatic microsomes as an alternative to the dog source for studying protein translocation

1995 ◽  
Vol 306 (1) ◽  
pp. 57-61 ◽  
Author(s):  
M A Kaderbhai ◽  
V J Harding ◽  
A Karim ◽  
B M Austen ◽  
N N Kaderbhai
Keyword(s):  
Protein Translocation ◽  
Membrane Vesicles ◽  
Heterologous Proteins

A procedure is described for the preparation of rough membrane vesicles of endoplasmic-reticular origin from the pancreas of sheep. These isolated membranes translocate, process and glycosylate in vitro-translated heterologous proteins in a manner comparable with that exhibited by dog pancreatic microsomes.

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