SecD and SecF are required for the proton electrochemical gradient stimulation of preprotein translocation.

Arkowitz, Robert A.; Wickner, William

doi:10.1002/j.1460-2075.1994.tb06340.x

Cited by 109 publications

(108 citation statements)

References 80 publications

Supporting

Mentioning

100

Contrasting

Unclassified

Order By: Relevance

“…The latter function is compatible with the observation that SecD and SecF show similarity to secondary solute transporters Tseng et al, 1999). Notably, the previously suggested function of SecD and SecF in maintenance of the proton motive force (Arkowitz & Wickner, 1994) was recently refuted (Nouwen et al, 2001). Archaea lack a number of components that are pivotal for protein transport in bacteria or eukarya, including homologues of the bacterial YidC protein and the eukaryotic TRAM and Sec63 proteins.…”

Section: The Sec Pathwaymentioning

confidence: 99%

Protein transport in the halophilic archaeon Halobacterium sp. NRC-1: a major role for the twin-arginine translocation pathway?

Bolhuis

2002

Microbiology

View full text Add to dashboard Cite

Section: The Sec Pathwaymentioning

confidence: 99%

Protein transport in the halophilic archaeon Halobacterium sp. NRC-1: a major role for the twin-arginine translocation pathway?

Bolhuis

2002

Microbiology

View full text Add to dashboard Cite

“…It has been reported that the depletion of SecD and SecF perturbs, for an unknown reason, the generation of the proton motive force (Ap) in cells and membrane vesicles [15]. Ap is composed of an electrical component, Au?, and a chemical component, ApH.…”

Section: Depletion Of Secg Does Not Perturb the Generation Of The Promentioning

confidence: 99%

SecG plays a critical role in protein translocation in the absence of the proton motive force as well as at low temperature

1996

View full text Add to dashboard Cite

SecG is an integral membrane component of E. coli protein translocase. However, a discrepancy exists as to the importance of SecG for protein translocation at 37°C between cells and reconstituted proteoliposomes; protein translocation in AsecG cells is defective at 20°C but normal at 37°C, indicating that SecG is dispensable at 37°C, whereas SecG remarkably stimulates protein translocation into reconstituted proteoliposomes at 37°C. In this study, protein translocation into membrane vesicles containing or not containing SecG was examined in the presence and absence of the proton motive force at 37°C and 20°C. We found that the absence of the proton motive force renders protein translocation strongly dependent on SecG even at 37°C. Protein translocation into proteoliposomes in the absence of the proton motive force thus required SecG whereas that in cells, which always generate the proton motive force, did not.

show abstract

“…By probing the nearest neighbors of a translocating preprotein using photocross-linking, it has been suggested recently that SecA and SecY may constitute a preprotein channel (20), which was detected previously by electrophysiological methods (52). The other integral membrane proteins, SecD and SecF, are important for efficient protein secretion, since secD and secF null mutants are cold sensitive for growth and display severe protein export defects even at permissive temperatures (15,42), but their role in protein export remains poorly defined and controversial (3,21,29).…”

mentioning

confidence: 99%

SecA proteins of Bacillus subtilis and Escherichia coli possess homologous amino-terminal ATP-binding domains regulating integration into the plasma membrane

1995

View full text Add to dashboard Cite

The Bacillus subtilis secA homolog, div, was cloned and expressed at a variety of different levels in wild-type and secA mutant strains of Escherichia coli. Analysis of Div function showed that it could not substitute for SecA despite being present at a wide range of concentrations at or above the physiological level. Location of regions of functional similarity between the two proteins using div-secA chimeras revealed that only the amino-terminal ATP-binding domain of Div could functionally substitute for the corresponding region of SecA. The role of this domain was revealed by subcellular localization experiments that demonstrated that in both B. subtilis and E. coli Div had cytoplasmic, peripheral, and integral membrane distributions similar to those of its SecA homolog and that an intact ATP-binding domain was essential for regulating integration of this protein into the plasma membrane. These results suggest strongly that the previously observed cycle of membrane binding, insertion, and deinsertion of SecA protein (A. Economou and W. Wickner, Cell 78:835-843, 1994) is common to these two bacteria, and they demonstrate the importance of the conserved ATP-binding domain in promoting this cycle.The ability of bacteria of the genus Bacillus to secrete large quantities of protein into culture media combined with an advanced state of knowledge of the molecular genetics of Bacillus subtilis makes this organism an attractive host for the large-scale production of proteins by recombinant DNA techniques. Despite the wide-scale industrial usage of this organism, however, the molecular details of its protein secretion remained largely unknown until recently. In contrast, genetic and biochemical studies with Escherichia coli have facilitated the identification of components of a complex protein secretion apparatus and assignment of specific functions to certain components (48, 60). SecB and specific heat shock proteins have been shown to serve as cytosolic chaperones that bind preproteins and maintain them in an export-competent conformation (24, 61). SecA has been shown to be a soluble and membrane-associated ATPase that is essential for functional binding and translocation of preproteins across inverted inner membrane vesicles (7,10,27,38). It appears likely that SecA promotes entry of the preprotein into the membranous export machinery by binding to the signal peptide and mature portions of the preprotein and inserting itself into the inner membrane (2,13,21,22,28). SecA association with the inner membrane is complex: initial binding requires anionic phospholipids and a functional SecY protein, while subsequent penetration and traversal of the membrane involve localized unfolding of a portion of SecA (4,8,17,28,57). Membrane reconstitution studies have shown that the integral membrane protein complex SecY-SecE-SecG is essential for efficient in vitro protein translocation (1,5,6,11,16,37). By probing the nearest neighbors of a translocating preprotein using photocross-linking, it has been suggested recently that SecA...

show abstract

SecD and SecF are required for the proton electrochemical gradient stimulation of preprotein translocation.

Cited by 109 publications

References 80 publications

Protein transport in the halophilic archaeon Halobacterium sp. NRC-1: a major role for the twin-arginine translocation pathway?

Protein transport in the halophilic archaeon Halobacterium sp. NRC-1: a major role for the twin-arginine translocation pathway?

SecG plays a critical role in protein translocation in the absence of the proton motive force as well as at low temperature

SecA proteins of Bacillus subtilis and Escherichia coli possess homologous amino-terminal ATP-binding domains regulating integration into the plasma membrane

Contact Info

Product

Resources

About