In vivo evidence for the role of the epsilon subunit as an inhibitor of the proton-translocating ATPase of Escherichia coli
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SecD and SecF are required for the proton electrochemical gradient stimulation of preprotein translocationThe fungal vacuole: composition, function, and biogenesisKdpD and KdpE, proteins that control expression of the kdpABC operon, are members of the two-component sensor-effector class of regulatorsRespiration and the F₁Fo-ATPase enhance survival under acidic conditions in Escherichia coliAn alternative role of FoF1-ATP synthase in Escherichia coli: synthesis of thiamine triphosphate.Intragenic and intergenic suppression of the Escherichia coli ATP synthase subunit a mutation of Gly-213 to Asn: functional interactions between residues in the proton transport siteTemperature dependence of single molecule rotation of the Escherichia coli ATP synthase F1 sector reveals the importance of gamma-beta subunit interactions in the catalytic dwell.A rotor-stator cross-link in the F1-ATPase blocks the rate-limiting step of rotational catalysisIntergenic suppression of the gammaM23K uncoupling mutation in F0F1 ATP synthase by betaGlu-381 substitutions: the role of the beta380DELSEED386 segment in energy coupling.SecA protein, a peripheral protein of the Escherichia coli plasma membrane, is essential for the functional binding and translocation of proOmpA.Characterization of the H(+)-pumping F1F0 ATPase of Vibrio alginolyticusTranslocation can drive the unfolding of a preprotein domain.Purification and characterization of the N-terminal domain of ExeA: a novel ATPase involved in the type II secretion pathway of Aeromonas hydrophilaEvaluating the oligomeric state of SecYEG in preprotein translocase.Direct observation of stepped proteolipid ring rotation in E. coli F₀F₁-ATP synthase.The torque of rotary F-ATPase can unfold subunit gamma if rotor and stator are cross-linked.Interacting cytoplasmic loops of subunits a and c of Escherichia coli F1F0 ATP synthase gate H+ transport to the cytoplasm.Significance of αThr-349 in the catalytic sites of Escherichia coli ATP synthase.Inhibition of ATP hydrolysis by thermoalkaliphilic F1Fo-ATP synthase is controlled by the C terminus of the epsilon subunit.The regulatory C-terminal domain of subunit ε of F₀F₁ ATP synthase is dispensable for growth and survival of Escherichia coli.The beta subunit loop that couples catalysis and rotation in ATP synthase has a critical length.Construction and plasmid-borne complementation of strains lacking the epsilon subunit of the Escherichia coli F1F0 ATP synthaseAdaptation of Streptococcus mutans and Enterococcus hirae to acid stress in continuous cultureIn vivo membrane assembly of the E.coli polytopic protein, melibiose permease, occurs via a Sec-independent process which requires the protonmotive force.Aerobic Growth of Escherichia coli Is Reduced, and ATP Synthesis Is Selectively Inhibited when Five C-terminal Residues Are Deleted from the ϵ Subunit of ATP Synthase.Engineering rotor ring stoichiometries in the ATP synthase.Both an N-terminal 65-kDa domain and a C-terminal 30-kDa domain of SecA cycle into the membrane at SecYEG during translocationAsp residues of βDELSEED-motif are required for peptide binding in the Escherichia coli ATP synthaseDefective gamma subunit of ATP synthase (F1F0) from Escherichia coli leads to resistance to aminoglycoside antibiotics.Ribosome-binding sites and RNA-processing sites in the transcript of the Escherichia coli unc operonUse of lac fusions to measure in vivo regulation of expression of Escherichia coli proton-translocating ATPase (unc) genesGenes encoding the beta and epsilon subunits of the proton-translocating ATPase from Anabaena sp. strain PCC 7120.Electrochemical potential releases a membrane-bound secretion intermediate of maltose-binding protein in Escherichia coliIdentification of the betaTP site in the x-ray structure of F1-ATPase as the high-affinity catalytic site.Synthesis of a functional F0 sector of the Escherichia coli H+-ATPase does not require synthesis of the alpha or beta subunits of F1The gamma-subunit rotation and torque generation in F1-ATPase from wild-type or uncoupled mutant Escherichia coli.ATP synthesis without R210 of subunit a in the Escherichia coli ATP synthase.Roles of SecG in ATP- and SecA-dependent protein translocation.A functionally important hydrogen-bonding network at the betaDP/alphaDP interface of ATP synthase.The two rotor components of yeast mitochondrial ATP synthase are mechanically coupled by subunit delta.
P2860
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P2860
In vivo evidence for the role of the epsilon subunit as an inhibitor of the proton-translocating ATPase of Escherichia coli
description
1984 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1984 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1984
@ast
im Dezember 1984 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1984/12/01)
@sk
vědecký článek publikovaný v roce 1984
@cs
wetenschappelijk artikel (gepubliceerd op 1984/12/01)
@nl
наукова стаття, опублікована в грудні 1984
@uk
научни чланак (објављен 1984/12/01)
@sr
name
In vivo evidence for the role ...... ing ATPase of Escherichia coli
@ast
In vivo evidence for the role ...... ing ATPase of Escherichia coli
@en
In vivo evidence for the role ...... ing ATPase of Escherichia coli
@nl
type
label
In vivo evidence for the role ...... ing ATPase of Escherichia coli
@ast
In vivo evidence for the role ...... ing ATPase of Escherichia coli
@en
In vivo evidence for the role ...... ing ATPase of Escherichia coli
@nl
prefLabel
In vivo evidence for the role ...... ing ATPase of Escherichia coli
@ast
In vivo evidence for the role ...... ing ATPase of Escherichia coli
@en
In vivo evidence for the role ...... ing ATPase of Escherichia coli
@nl
P2093
P2860
P1476
In vivo evidence for the role ...... ing ATPase of Escherichia coli
@en
P2093
D J Klionsky
R D Simoni
W S Brusilow
P2860
P304
P407
P577
1984-12-01T00:00:00Z