Identification of a Region of Interaction between Escherichia coli SecA and SecY Proteins

Snyders, Shaun; Ramamurthy, Visvanathan; Oliver, Donald B.

doi:10.1074/jbc.272.17.11302

Cited by 69 publications

(95 citation statements)

References 45 publications

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“…When SecA interacts with SecY 48,49 through its Nterminal 37 and/or C-terminal domain, 50 there is an increase in ATP-driven proteolytic stability 13 that is fundamentally different from what is observed when SecA binds ATP in solution. 39 Interestingly, there is also evidence that interaction between SecA and SecYEG changes the oligomeric structure of SecYEG.…”

Section: Discussionmentioning

confidence: 99%

The ATPase domain of SecA can form a tetramer in solution 1 1Edited by I. B. Holland

Dempsey

Economou

Dunn

et al. 2002

Journal of Molecular Biology

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Section: Discussionmentioning

confidence: 99%

The ATPase domain of SecA can form a tetramer in solution 1 1Edited by I. B. Holland

Dempsey

Economou

Dunn

et al. 2002

Journal of Molecular Biology

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“…5) Mutations in secY encoding intramembrane and periplasmic regions show allele-specific genetic interaction with secA and profoundly influence the SecA cycle of membrane insertion and deinsertion (40). 6) SecA can interact with SecY fragments that originate from a transmembrane region (41).…”

Section: An Intact Membrane Is Required For Full Protease Resistance mentioning

confidence: 99%

Endogenous SecA Catalyzes Preprotein Translocation at SecYEG

Eichler¹,

Rinard

Wickner

1998

Journal of Biological Chemistry

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SecA is found in the cytosol and bound to the plasma membrane of Escherichia coli. Binding occurs either with high affinity at SecYEG or with low affinity to lipid. Domains of 65 and 30 kDa of SecYEG-bound SecA insert into the membrane upon interaction with preprotein and ATP. Azide blocks preprotein translocation, in vivo and in vitro, through interacting with SecA and preventing SecA deinsertion. This provides a measure of the translocation relevance of each form of SecA membrane association. We now report that azide acts exclusively on SecA that is cycling at SecYEG and has no effect on SecA lipid associations. SecA molecules recovered with sucrose gradient-purified inner membrane vesicles ("endogenous" SecA) support translocation at the same rate as "added" SecA molecules bound at SecYEG. Both endogenous and added SecA yield the same proteolytic fragments, which are distinct from those obtained from SecA once it has inserted into membranes at SecYEG or from SecA at lipidic sites. Endogenous and added SecA differ, however, in their resistance to urea extraction. The translocation supported by either endogenous or added SecA is blocked by azide or by antibody to SecY. We conclude that SecA functions in preprotein translocation only through cycling at SecYEG.

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“…SecA plays a central role as it is the site of preprotein entry into the translocase, is the only ATPase essential for preprotein translocation, and interacts with most of the other Sec-proteins (reviewed in [1*]). SecA is present in the cell in large excess of the other Sec-proteins and binds with a high affinity to SecY [16"*, [17][18][19].…”

Section: Preprotein Translocation Across the Membranementioning

confidence: 99%

The Sec system

Driessen

Fekkes

Wolk

1998

Current Opinion in Microbiology

159

111

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The Sec system Driessen, A.J.M.; Fekkes, P.; van der Wolk, J.P.W. Take-down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim.Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal. For technical reasons the number of authors shown on this cover page is limited to 10 maximum. Proteins designated to be secreted by Escherichia coil are synthesized with an amino-terminal signal peptide and associate as nascent chains with the export-specific chaperone SecB. Translocation occurs at a multisubunit membrane-bound enzyme termed translocase, which consists of a peripheral preprotein-binding site and an ATPase domain termed SecA, a core heterotrimeric integral membrane protein complex with SecY, SecE and SecG as subunits, and an accessory integral membrane protein complex containing SecD and SecE Major new insights have been gained into the cascade of preprotein targeting events and the enzymatic mechanism of preprotein translocation. It has become clear that preproteins are translocated in a stepwise fashion involving large nucleotide-induced conformational changes of the molecular motor SecA that propels the translocation reaction. Addresses

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Identification of a Region of Interaction between Escherichia coli SecA and SecY Proteins

Cited by 69 publications

References 45 publications

The ATPase domain of SecA can form a tetramer in solution 1 1Edited by I. B. Holland

The ATPase domain of SecA can form a tetramer in solution 1 1Edited by I. B. Holland

Endogenous SecA Catalyzes Preprotein Translocation at SecYEG

The Sec system

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