ProOmpA spontaneously folds in a membrane assembly competent state which trigger factor stabilizes.
about
SecD and SecF are required for the proton electrochemical gradient stimulation of preprotein translocationThe complete general secretory pathway in gram-negative bacteriaSecA protein, a peripheral protein of the Escherichia coli plasma membrane, is essential for the functional binding and translocation of proOmpA.SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli.Three pure chaperone proteins of Escherichia coli--SecB, trigger factor and GroEL--form soluble complexes with precursor proteins in vitro.Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme.Sec-dependent membrane protein biogenesis: SecYEG, preprotein hydrophobicity and translocation kinetics control the stop-transfer function.A role for trigger factor and an rgg-like regulator in the transcription, secretion and processing of the cysteine proteinase of Streptococcus pyogenes.The PrlA and PrlG phenotypes are caused by a loosened association among the translocase SecYEG subunits.ProOmpA contains secondary and tertiary structure prior to translocation and is shielded from aggregation by association with SecB proteinInteractive surface in the PapD chaperone cleft is conserved in pilus chaperone superfamily and essential in subunit recognition and assembly.Translocation can drive the unfolding of a preprotein domain.Sec-dependent protein export and the involvement of the molecular chaperone SecB.Trigger factor depletion or overproduction causes defective cell division but does not block protein export.Specific recognition of the leader region of precursor proteins is required for the activation of translocation ATPase of Escherichia coli.Detergent disruption of bacterial inner membranes and recovery of protein translocation activity.Physiological role during export for the retardation of folding by the leader peptide of maltose-binding protein.Evaluating the oligomeric state of SecYEG in preprotein translocase.Multitasking SecB chaperones in bacteriaProbing the SecYEG translocation pore size with preproteins conjugated with sizable rigid spherical molecules.Trigger factor-mediated prolyl isomerization influences maturation of the Streptococcus pyogenes cysteine protease.A little help from my friends: quality control of presecretory proteins in bacteriaBoth an N-terminal 65-kDa domain and a C-terminal 30-kDa domain of SecA cycle into the membrane at SecYEG during translocationThe folding properties of the Escherichia coli maltose-binding protein influence its interaction with SecB in vitro.Temperature-dependent insertion of prolipoprotein into Escherichia coli membrane vesicles and requirements for ATP, soluble factors, and functional SecY protein for the overall translocation process.In vitro insertion of leader peptidase into Escherichia coli membrane vesicles.Electrochemical potential releases a membrane-bound secretion intermediate of maltose-binding protein in Escherichia coliRoles of SecG in ATP- and SecA-dependent protein translocation.Insertion of proteins into bacterial membranes: mechanism, characteristics, and comparisons with the eucaryotic process.Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides.Escherichia coli sec mutants accumulate a processed immature form of maltose-binding protein (MBP), a late-phase intermediate in MBP export.Investigating the SecY plug movement at the SecYEG translocation channel.Preprotein translocation by a hybrid translocase composed of Escherichia coli and Bacillus subtilis subunits.A mutation in secY that causes enhanced SecA insertion and impaired late functions in protein translocation.Molybdenum requirement for translocation of dimethyl sulfoxide reductase to the periplasmic space in a photodenitrifier, Rhodobacter sphaeroides f. sp. denitrificans.A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor.The precursor of beta-lactamase: purification, properties and folding kinetics.Effects of mutations in heat-shock genes groES and groEL on protein export in Escherichia coli.Signal recognition particle (SRP) stabilizes the translocation-competent conformation of pre-secretory proteinsThe Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor
P2860
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P2860
ProOmpA spontaneously folds in a membrane assembly competent state which trigger factor stabilizes.
description
1988 nî lūn-bûn
@nan
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
1988年论文
@zh
1988年论文
@zh-cn
name
ProOmpA spontaneously folds in ...... ich trigger factor stabilizes.
@en
type
label
ProOmpA spontaneously folds in ...... ich trigger factor stabilizes.
@en
prefLabel
ProOmpA spontaneously folds in ...... ich trigger factor stabilizes.
@en
P2093
P2860
P1433
P1476
ProOmpA spontaneously folds in ...... ich trigger factor stabilizes.
@en
P2093
P2860
P304
P407
P577
1988-06-01T00:00:00Z