A mutation affecting the regulation of a secA-lacZ fusion defines a new sec gene.
about
SecD and SecF are required for the proton electrochemical gradient stimulation of preprotein translocationThe Sec-dependent pathwaySelective ribosome profiling reveals the cotranslational chaperone action of trigger factor in vivoKinetic analysis of the assembly of the outer membrane protein LamB in Escherichia coli mutants each lacking a secretion or targeting factor in a different cellular compartment.Characterization of the Cpx regulon in Escherichia coli strain MC4100.Genomics and antimicrobial drug discovery.SecA suppresses the temperature-sensitive SecY24 defect in protein translocation in Escherichia coli membrane vesicles.Revised translation start site for secM defines an atypical signal peptide that regulates Escherichia coli secA expression.Peculiar properties of DsbA in its export across the Escherichia coli cytoplasmic membraneAzide-resistant mutants of Escherichia coli alter the SecA protein, an azide-sensitive component of the protein export machinery.The secD locus of E.coli codes for two membrane proteins required for protein export.Oversynthesis of a new Escherichia coli small RNA suppresses export toxicity of DsbA'-PhoA unfoldable periplasmic proteins.The Cs sec mutants of Escherichia coli reflect the cold sensitivity of protein export itself.Lon protease quality control of presecretory proteins in Escherichia coli and its dependence on the SecB and DnaJ (Hsp40) chaperones.Modeling the effects of prl mutations on the Escherichia coli SecY complex.A novel membrane protein involved in protein translocation across the cytoplasmic membrane of Escherichia coli.Genetic screen yields mutations in genes encoding all known components of the Escherichia coli signal recognition particle pathway.Detergent disruption of bacterial inner membranes and recovery of protein translocation activity.A novel class of secA alleles that exert a signal-sequence-dependent effect on protein export in Escherichia coli.A cytoplasmic domain is important for the formation of a SecY-SecE translocator complex.An essential amino acid residue in the protein translocation channel revealed by targeted random mutagenesis of SecYOne of three transmembrane stretches is sufficient for the functioning of the SecE protein, a membrane component of the E. coli secretion machinery.A mutation of Escherichia coli SecA protein that partially compensates for the absence of SecB.Genetic and molecular characterization of the Escherichia coli secD operon and its productsExport of the outer membrane lipoprotein is defective in secD, secE, and secF mutants of Escherichia coli.Regions of maltose-binding protein that influence SecB-dependent and SecA-dependent export in Escherichia coliIsolation and analysis of dominant secA mutations in Escherichia coliRegulation of Escherichia coli secA mRNA translation by a secretion-responsive element.The first gene in the Escherichia coli secA operon, gene X, encodes a nonessential secretory proteinNovel secA alleles improve export of maltose-binding protein synthesized with a defective signal peptide.SecA protein autogenously represses its own translation during normal protein secretion in Escherichia coli.The mature portion of Escherichia coli maltose-binding protein (MBP) determines the dependence of MBP on SecB for export.Characterization of cold-sensitive secY mutants of Escherichia coliSecA protein is required for translocation of a model precursor protein into inverted vesicles of Escherichia coli plasma membrane.Insertion of proteins into bacterial membranes: mechanism, characteristics, and comparisons with the eucaryotic process.Rational elicitation of cold-sensitive phenotypes.Genetic suppressors and recovery of repressed biochemical memory.A new genetic selection identifies essential residues in SecG, a component of the Escherichia coli protein export machineryDisruption of the gene encoding p12 (SecG) reveals the direct involvement and important function of SecG in the protein translocation of Escherichia coli at low temperature.Reconstitution of protein translocation from detergent-solubilized Escherichia coli inverted vesicles: PrlA protein-deficient vesicles efficiently translocate precursor proteins
P2860
Q24596484-0F50D87B-EE49-4DE0-B942-405DC71C1F9FQ27010633-9EA858DD-D605-4315-BEBB-ECC0CB1C9045Q30155411-11576D0D-795A-45FB-BA6C-EBECA7BA2944Q30159588-75CC91DC-04BB-42FA-BCF7-3CDDA786DE4CQ33395214-6E14E9E3-1716-4DB0-8A2E-993765B9F192Q33537162-DD24BE3B-8705-4147-A66B-7DAD71496FD1Q33677536-B6FFD384-02B5-44FC-8D95-C65FF1E23F1FQ33787527-0216EAFB-BA39-47A8-A18E-CF1206D4C985Q33855584-348238F4-9FDC-4131-AE1C-C412C07F3E70Q33858303-DAE93E5E-24AE-4BCD-BA2B-258D84DFFC71Q33922088-D09B7531-120B-4BBF-B9C9-133ADDB4B76CQ33931330-BFE7E27E-2A61-4ABE-9F41-9953363E5DB4Q33960682-F4014436-681C-4AB8-90DC-99ADA8D7FBC8Q34004070-6C508E77-2CC7-4BAC-B753-B03B2FBA0684Q34048338-1E4B2A53-7C75-4757-8842-65A9EB3B75AEQ34058655-BD2F823D-4D0D-4F42-B297-25A3B1B878ECQ34304210-80169400-5B44-4608-8E85-32254EB2B078Q34318277-BBDE25F9-AF21-4969-B47E-8706D09E5C2BQ34616261-F8317550-FB3F-45A6-B391-107E1D5BB6B5Q35241622-B4B79010-0F57-486D-8818-76211400A1BEQ35865651-E0EB0A5B-854A-4B25-86CF-82BDC85FC016Q35926815-D6873D10-3477-40BF-A503-F89F56EA3AB9Q36098219-ADF1256C-9198-4C52-83EE-2CA99038EA58Q36105112-E68E0E84-2EF1-4946-A17C-2EEB63BFCD44Q36110909-83FE9B96-89EA-496D-8B9C-113FF4F8CA1DQ36123480-88B45C41-02ED-4E13-A3AB-505A157CB6B8Q36125831-269C53E8-EEA3-42F2-85DA-24B4B54A9C10Q36163727-FB3D9C4D-8E3A-423C-9884-A5FBC0654EC6Q36165846-B457F3C1-81AF-4E3D-803D-2971A38EB1BFQ36173206-1F0FA3C3-AD4D-4BA0-8E69-65B2CB116B63Q36173585-B91D84A6-3D78-402B-983E-CEBFB45924F9Q36174105-4BD186DD-C57C-4BA7-BB7F-D85AD26043A2Q36192541-E812E36C-049A-42C0-9C1A-223EB1CE3564Q36567392-ABE45897-2170-4A2C-A836-8B543FF7F5FBQ37055727-79246702-916A-41E2-A790-E11350F05E7DQ37173130-B4E58E19-007D-4B09-BA96-F31225CB5FD9Q37364322-C48FEEB2-FB94-4AE5-9638-97978F6B6221Q37622554-DADEC09B-C02E-4262-B208-F6F972E8767EQ37634521-EE978CA4-C64D-4CA9-89CF-7087D59E6260Q37714073-62224475-C4AE-4CFF-9A7E-04888B482659
P2860
A mutation affecting the regulation of a secA-lacZ fusion defines a new sec gene.
description
1988 nî lūn-bûn
@nan
1988 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1988 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
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
name
A mutation affecting the regulation of a secA-lacZ fusion defines a new sec gene.
@ast
A mutation affecting the regulation of a secA-lacZ fusion defines a new sec gene.
@en
type
label
A mutation affecting the regulation of a secA-lacZ fusion defines a new sec gene.
@ast
A mutation affecting the regulation of a secA-lacZ fusion defines a new sec gene.
@en
prefLabel
A mutation affecting the regulation of a secA-lacZ fusion defines a new sec gene.
@ast
A mutation affecting the regulation of a secA-lacZ fusion defines a new sec gene.
@en
P2093
P2860
P1433
P1476
A mutation affecting the regulation of a secA-lacZ fusion defines a new sec gene
@en
P2093
P2860
P304
P407
P577
1988-04-01T00:00:00Z