Journal ArticleDOI
The ATPase activity of secA is regulated by acidic phospholipids, secY, and the leader and mature domains of precursor proteins
TLDR
This work defines the stimulation of SecA ATPase by lipid as "SecA/lipid ATPase", and indicates that liposome-bound SecA protein recognizes both leader and mature domains, suggesting an underlying unity of mechanism.About:
This article is published in Cell.The article was published on 1990-01-26. It has received 553 citations till now. The article focuses on the topics: SecY protein & ATPase.read more
Citations
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The complete general secretory pathway in gram-negative bacteria
TL;DR: The unifying feature of all proteins that are transported out of the cytoplasm of gram-negative bacteria by the general secretory pathway is the presence of a long stretch of predominantly hydrophobic amino acids, the signal sequence.
Journal ArticleDOI
MOLECULAR BASIS FOR MEMBRANE PHOSPHOLIPID DIVERSITY: Why Are There So Many Lipids?
TL;DR: The wide range of processes in which specific involvement of phospholipids has been documented explains the need for diversity inospholipid structure and why there are so many membrane lipids.
Journal ArticleDOI
Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
TL;DR: Structural, genetic and biochemical data show how the channel opens across the membrane, releases hydrophobic segments of membrane proteins laterally into lipid, and maintains the membrane barrier for small molecules.
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Signal Peptide-Dependent Protein Transport in Bacillus subtilis : a Genome-Based Survey of the Secretome
TL;DR: The predictions and comparisons in this review pinpoint important differences as well as similarities between protein transport systems in B. subtilis and other well-studied organisms, such as Escherichia coli and the yeast Saccharomyces cerevisiae, which may serve as a lead for future research and applications.
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Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate
TL;DR: Folding of two monomeric enzymes mediated by groE has been reconstituted in vitro and might represent a general mechanism for the formation of protein structure in vivo.
References
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Journal ArticleDOI
Patterns of Amino Acids near Signal‐Sequence Cleavage Sites
TL;DR: In this paper, some such patterns, based on a sample of 78 eukaryotic signal sequences, are presented and discussed, and a first attempt at formulating rules for the prediction of cleavage sites is made.
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An improved assay for nanomole amounts of inorganic phosphate
TL;DR: This method (through the use of a citratelarsenite mixture added immediately after the molybdate reagent) is relatively sensitive, color stable, and has the advantage of being insensitive to any newly released phosphate.
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A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides
Raymond J. Deshaies,Bruce D. Koch,Margaret Werner-Washburne,Elizabeth A. Craig,Randy Schekman +4 more
TL;DR: Depletion of a subset of 7OK stress proteins in yeast mutants shows that they are involved in the post-translational import of precursor polypeptides into both mitochondria and the lumen of the endoplasmic reticulum.
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Homologous plant and bacterial proteins chaperone oligomeric protein assembly
Sean M. Hemmingsen,Carol A. Woolford,Saskia M. van der Vies,Kit Tilly,David T. Dennis,Costa Georgopoulos,Roger W. Hendrix,R. John Ellis +7 more
TL;DR: Chaperonins comprise a class of molecular chaperones that are found in chloroplasts, mitochondria and prokaryotes and are implicated in the assembly of the oligomeric enzyme ribulose bisphosphate carboxylase-oxygenase, which catalyses photosynthetic CO2-fixation in higher plants.
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70K heat shock related proteins stimulate protein translocation into microsomes
TL;DR: A yeast cytosol is shown to contain two distinct activities that stimulate protein translocation across microsomal membranes that increase the rate of translocation.