SecA, a novel ATPase that converts chemical energy into a mechanical force to drive precursor protein translocation

Driessen, Arnold J.M.; Wit, de Janny; Kuiper, W.; Wolk, J.P.W. van der; Fekkes, Peter; Does, Chris van der; Wely, Karel H. M. van; Manting, Erik H.; Blaauwen, Tanneke den

doi:10.1042/bst0230981

Cited by 13 publications

(7 citation statements)

References 5 publications

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“…The subcellular distribution of FtsY is reminiscent of SecA, which is also a nucleotide binding protein and does not contain hydrophobic transmembrane sequences [22]. SecA is a translocon component that has affinity both for membrane lipids and the integral translocon component SecY (reviewed in [27]). Recent evidence indicates that SecA shuttles between a membrane inserted and de‐inserted state, a process that is regulated by ATP binding and hydrolysis [28].…”

Section: Discussionmentioning

confidence: 99%

Membrane association of FtsY, the E. coli SRP receptor

Leeuw¹,

Poland²,

Mol

et al. 1997

FEBS Letters

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FtsY, the Escherichia coli homologue of the eukaryotic SRP receptor (SRa), is located both in the cytoplasm and in the inner membrane of E. coli. Similar to SRa, FtsY consists of two major domains: a strongly acidic N-terminal domain (A) and a C-terminal GTP binding domain (NG) of which the crystal structure has recently been determined. The domains were expressed both in vivo and in vitro to examine their subcellular localization. The results suggest that both domains associate with the membrane but that the nature of the association differs.

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Section: Discussionmentioning

confidence: 99%

Membrane association of FtsY, the E. coli SRP receptor

Leeuw¹,

Poland²,

Mol

et al. 1997

FEBS Letters

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“…Upon binding of the SecB ⁄ ProOmpA complex to the C terminus of SecA, stepwise translocation of unfolded ProOmpA across the membrane is driven by the ATPase activity of SecA and the proton-motive force [58]. At the outer leaflet of the inner membrane, the signal sequence is cleaved off by signal peptidase [59] (Fig.…”

Section: Translocation From the Ribosome To The Periplasmmentioning

confidence: 99%

Insights into the structure and assembly of Escherichia coli outer membrane protein A

Reusch

2012

The FEBS Journal

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Outer membrane protein A (OmpA) of Escherichia coli is a paradigm for the biogenesis of outer membrane proteins; however, the structure and assembly of OmpA have remained controversial. A review of studies to date supports the hypothesis that native OmpA is a single-domain large pore, while a two-domain narrow pore structure is a folding intermediate or minor conformer. The in vitro refolding of OmpA to the large pore conformation requires that the protein be isolated from outer membranes with an intact disulfide bond and then adequately incubated in lipids at temperatures ≥ 26 °C to overcome the high energy of activation for refolding. The in vivo maturation of the protein involves covalent modification of serines in the eighth β-barrel of the N-terminal domain by oligo-(R)-3-hydroxybutyrates as the protein is escorted across the cytoplasm by SecB for post-translational secretion across the SEC translocase in the inner membrane. After cleavage of the signal sequence, protein chaperones, such a Skp, DegP and SurA, guide OmpA across the periplasm to the BAM complex in the outer membrane. During this passage, a disulfide bond is formed between C290 and C302 by DsbA, and the hydrophobicity of segments of the C-terminal domain which are destined for incorporation as β-barrels in the outer membrane bilayer is increased by covalent attachment of oligo-(R)-3-hydroxybutyrates. With the aid of the BAM complex, OmpA is then assembled into the outer membrane as a single-domain large pore.

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“…By doing so, SecB prevents premature folding and aggregation of the newly synthesized preprotein (Kusters et al, 1989;Lecker et al, 1989) and also pilots the preproteins to the peripheral translocon component SecA (Hartl et al, 1990). SecA is an ATPase that has affinity not only for SecB but also for the attached preprotein and for the integral translocon subunit SecY (reviewed in Driessen et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

Nascent membrane and presecretory proteins synthesized in Escherichia coli associate with signal recognition particle and trigger factor

Valent¹,

Gier

Heijne

et al. 1997

Molecular Microbiology

164

187

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SummaryThe Escherichia coli signal recognition particle (SRP) and trigger factor are cytoplasmic factors that interact with short nascent polypeptides of presecretory and membrane proteins produced in a heterologous in vitro translation system. In this study, we use an E. coli in vitro translation system in combination with bifunctional cross-linking reagents to investigate these interactions in more detail in a homologous environment. Using this approach, the direct interaction of SRP with nascent polypeptides that expose particularly hydrophobic targeting signals is demonstrated, suggesting that inner membrane proteins are the primary physiological substrate of the E. coli SRP. Evidence is presented that the overproduction of proteins that expose hydrophobic polypeptide stretches, titrates SRP. In addition, trigger factor is efficiently cross-linked to nascent polypeptides of different length and nature, some as short as 57 amino acid residues, indicating that it is positioned near the nascent chain exit site on the E. coli ribosome.

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SecA, a novel ATPase that converts chemical energy into a mechanical force to drive precursor protein translocation

Cited by 13 publications

References 5 publications

Membrane association of FtsY, the E. coli SRP receptor

Membrane association of FtsY, the E. coli SRP receptor

Insights into the structure and assembly of Escherichia coli outer membrane protein A

Nascent membrane and presecretory proteins synthesized in Escherichia coli associate with signal recognition particle and trigger factor

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