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Literature DB >> 14597695

SecA-dependent quality control of intracellular protein localization.

Abstract

Complex secretion machineries mediate protein translocation across cellular membranes. These machines typically recognize their substrates via signal sequences, which are required for proper targeting to the translocon. We report that during posttranslational secretion the widely conserved targeting factor SecA performs a quality-control function that is based on a general chaperone activity. This quality-control mechanism involves assisted folding of signal sequenceless proteins, thereby excluding them from the secretion process. These results suggest that SecA channels proteins into one of two key pathways, posttranslational secretion or folding in the cytoplasm. Implications of this finding for intracellular protein localization are discussed.

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Year: 2003 PMID： 14597695 PMCID： PMC263763 DOI： 10.1073/pnas.2234410100

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

22 in total

1. Allosteric communication between signal peptides and the SecA protein DEAD motor ATPase domain.

Authors: Catherine Baud; Spyridoula Karamanou; Giorgos Sianidis; Eleftheria Vrontou; Anastasia S Politou; Anastassios Economou
Journal: J Biol Chem Date: 2002-02-01 Impact factor: 5.157

Review 2. The Sec protein-translocation pathway.

Authors: H Mori; K Ito
Journal: Trends Microbiol Date: 2001-10 Impact factor: 17.079

3. Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase.

Authors: Vivek Sharma; Arulandu Arockiasamy; Donald R Ronning; Christos G Savva; Andreas Holzenburg; Miriam Braunstein; William R Jacobs; James C Sacchettini
Journal: Proc Natl Acad Sci U S A Date: 2003-02-26 Impact factor: 11.205

Review 4. Protein translocons: multifunctional mediators of protein translocation across membranes.

Authors: Danny J Schnell; Daniel N Hebert
Journal: Cell Date: 2003-02-21 Impact factor: 41.582

5. Determination of a region in SecA that interacts with presecretory proteins in Escherichia coli.

Authors: E Kimura; M Akita; S Matsuyama; S Mizushima
Journal: J Biol Chem Date: 1991-04-05 Impact factor: 5.157

Review 6. Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes.

Authors: T A Rapoport; B Jungnickel; U Kutay
Journal: Annu Rev Biochem Date: 1996 Impact factor: 23.643

7. Does secA mediate coupling between secretion and translation in Escherichia coli?

Authors: K L Strauch; C A Kumamoto; J Beckwith
Journal: J Bacteriol Date: 1986-05 Impact factor: 3.490

8. Modulation of folding pathways of exported proteins by the leader sequence.

Authors: S Park; G Liu; T B Topping; W H Cover; L L Randall
Journal: Science Date: 1988-02-26 Impact factor: 47.728

9. E. coli mutant pleiotropically defective in the export of secreted proteins.

Authors: D B Oliver; J Beckwith
Journal: Cell Date: 1981-09 Impact factor: 41.582

10. Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma.

Authors: G Blobel; B Dobberstein
Journal: J Cell Biol Date: 1975-12 Impact factor: 10.539

14 in total

Review 10. SecA, a remarkable nanomachine.

Authors: Ilja Kusters; Arnold J M Driessen
Journal: Cell Mol Life Sci Date: 2011-04-10 Impact factor: 9.261

SecA-dependent quality control of intracellular protein localization.

1. Allosteric communication between signal peptides and the SecA protein DEAD motor ATPase domain.

Review 2. The Sec protein-translocation pathway.

3. Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase.

Review 4. Protein translocons: multifunctional mediators of protein translocation across membranes.

5. Determination of a region in SecA that interacts with presecretory proteins in Escherichia coli.

Review 6. Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes.

7. Does secA mediate coupling between secretion and translation in Escherichia coli?

8. Modulation of folding pathways of exported proteins by the leader sequence.

9. E. coli mutant pleiotropically defective in the export of secreted proteins.

10. Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma.

Review 1. Interactions that drive Sec-dependent bacterial protein transport.

2. Target-directed proteolysis at the ribosome.

Review 3. A little help from my friends: quality control of presecretory proteins in bacteria.

Review 4. Oligomeric states of the SecA and SecYEG core components of the bacterial Sec translocon.

Review 5. SecA: a potential antimicrobial target.

6. Protein export by the mycobacterial SecA2 system is determined by the preprotein mature domain.

7. The Tat Substrate CueO Is Transported in an Incomplete Folding State.

8. Trigger factor is a bona fide secretory pathway chaperone that interacts with SecB and the translocase.

9. SecB is a bona fide generalized chaperone in Escherichia coli.

Review 10. SecA, a remarkable nanomachine.