Precursor-specific requirements for SecA, SecB, and delta muH+ during protein export of Escherichia coli.

Ernst, Friedrich; Hoffschulte, Hedda K.; Thome-Kromer, B; Swidersky, Ulla E.; Werner, Pamela K.; Müller, Matthias

doi:10.1016/s0021-9258(18)99952-7

Cited by 25 publications

(4 citation statements)

References 45 publications

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“…Though the cpSec machinery has not received as much attention, SecA, SecY, and SecE protein homologues exist in higher plant plastids (7)(8)(9). ATP hydrolysis by SecA is essential for Sec transport, yet a proton motive force (pmf) 1 improves transport rate and energetic efficiency (2,(10)(11)(12)(13)(14). SecA is responsible for initiation of translocation, a task accomplished through major conformational changes resulting in the insertion of two large SecA domains (30 and 65 kDa) into the translocase with the bound leader sequence (15,16).…”

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confidence: 99%

“…The pmf also drives later steps of translocation in the absence of SecA and ATP hydrolysis. The exact roles of the ∆ψ and ∆pH components of the pmf in these later steps of precursor translocation have not been deciphered as they are precursor protein dependent, although ∆ψ-driven electrophoretic movement appears to be utilized in some cases (11,13,(19)(20)(21)(22)(23)(24). Note that it is unlikely that a ∆ψ plays a role in cpSec transport due to the low steady-state ∆ψ maintained across the thylakoid membrane in the light (25).…”

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confidence: 99%

“…While the decrease in ∆pH observed during translocation initiation in bacteria (26) could be explained by simple leakage resulting from the presence of a large protein molecule within the translocation pore, no model has yet been proposed to explain the decreased translocation rate observed in D 2 O (27), a result that supports a direct role for rate-limiting proton transfer in ∆pH-driven translocation. A tightly coupled protein/proton antiporter activity is an enticing possibility, although it is difficult to reconcile with the observed protein dependence of pmf stimulated transport (11,(21)(22)(23).…”

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confidence: 99%

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Proton Transfer Limits Protein Translocation Rate by the Thylakoid ΔpH/Tat Machinery

Musser¹,

Theg²

2000

Biochemistry

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The thylakoid transmembrane DeltapH is the sole energy source driving translocation of precursor proteins by the DeltapH/Tat machinery. Consequently, proton translocation must be coupled to precursor translocation. For the precursor of the 17 kDa protein of the oxygen-evolving complex (pOE17), the protein translocation process is characterized by a steep drop in efficiency at an external pH below 7.0 and above 8.7. As the membrane DeltapH is virtually unaffected from pH 6.5 to 9.2, the loss in import efficiency is a consequence of the titration of multiple residues within the translocation machinery. Transport is retarded by a factor of 2-3 in deuterium oxide (D(2)O) relative to water, strongly suggesting that proton-transfer reactions limit translocation rate. The solvent isotope effect manifests itself after the precursor binds to the membrane, indicating that the rate-limiting step is a later event in the transport process.

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Proton Transfer Limits Protein Translocation Rate by the Thylakoid ΔpH/Tat Machinery

Musser¹,

Theg²

2000

Biochemistry

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“…The OMP is first translated on the ribosome into a nascent polypeptide that does not have biological functions, that is, OMP precursors, and its N-terminus has signal peptides. The signal peptide can be recognized by the Sec translocation system, and pass through the inner membrane to the periplasmic space (Figure 2) [55][56][57][58][59]. Next, signal peptidase recognizes and excises the signal peptide at the N-terminus of the OMP precursor.…”

Section: Folding and Insertion Of Omps By The Bam Complexmentioning

confidence: 99%

β-Barrel Assembly Machinery (BAM) Complex as Novel Antibacterial Drug Target

Guo

2023

Molecules

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The outer membrane of Gram-negative bacteria is closely related to the pathogenicity and drug resistance of bacteria. Outer membrane proteins (OMPs) are a class of proteins with important biological functions on the outer membrane. The β-barrel assembly machinery (BAM) complex plays a key role in OMP biogenesis, which ensures that the OMP is inserted into the outer membrane in a correct folding manner and performs nutrient uptake, antibiotic resistance, cell adhesion, cell signaling, and maintenance of membrane stability and other functions. The BAM complex is highly conserved among Gram-negative bacteria. The abnormality of the BAM complex will lead to the obstruction of OMP folding, affect the function of the outer membrane, and eventually lead to bacterial death. In view of the important role of the BAM complex in OMP biogenesis, the BAM complex has become an attractive target for the development of new antibacterial drugs against Gram-negative bacteria. Here, we summarize the structure and function of the BAM complex and review the latest research progress of antibacterial drugs targeting BAM in order to provide a new perspective for the development of antibiotics.

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Thylakoidal Protein Transport by the Sec-Dependent Pathway: The Involvement of ΔPH

Mant¹,

Robinson²

1995

Photosynthesis: From Light to Biosphere

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Precursor-specific requirements for SecA, SecB, and delta muH+ during protein export of Escherichia coli.

Cited by 25 publications

References 45 publications

Proton Transfer Limits Protein Translocation Rate by the Thylakoid ΔpH/Tat Machinery

Proton Transfer Limits Protein Translocation Rate by the Thylakoid ΔpH/Tat Machinery

β-Barrel Assembly Machinery (BAM) Complex as Novel Antibacterial Drug Target

Thylakoidal Protein Transport by the Sec-Dependent Pathway: The Involvement of ΔPH

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