GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation
about
Getting on target: the archaeal signal recognition particlePrediction of signal recognition particle RNA genes.p190 RhoGAP, the major RasGAP-associated protein, binds GTP directlyThe signal recognition particle (SRP) RNA links conformational changes in the SRP to protein targetingThe beta subunit of the signal recognition particle receptor is a transmembrane GTPase that anchors the alpha subunit, a peripheral membrane GTPase, to the endoplasmic reticulum membraneThe ribosome regulates the GTPase of the beta-subunit of the signal recognition particle receptorThe conformation of bound GMPPNP suggests a mechanism for gating the active site of the SRP GTPaseStructure of the GMPPNP-stabilized NG domain complex of the SRP GTPases Ffh and FtsYCrystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communicationNovel protein and Mg2+ configurations in the Mg2+GDP complex of the SRP GTPase ffhHeterodimeric GTPase Core of the SRP Targeting ComplexThe yeast nascent polypeptide-associated complex initiates protein targeting to mitochondria in vivo.A functional GTPase domain, but not its transmembrane domain, is required for function of the SRP receptor beta-subunit.Subunits of the Saccharomyces cerevisiae signal recognition particle required for its functional expression.The beta-subunit of the protein-conducting channel of the endoplasmic reticulum functions as the guanine nucleotide exchange factor for the beta-subunit of the signal recognition particle receptor.Evidence for a novel GTPase priming step in the SRP protein targeting pathway.A complex of the signal sequence binding protein and the SRP RNA promotes translocation of nascent proteinsMolecular evolution of SRP cycle components: functional implicationsMembrane topology and insertion of membrane proteins: search for topogenic signalsUse of synthetic signal sequences to explore the protein export machinery.Protein targeting to the bacterial cytoplasmic membrane.High-affinity binding of Escherichia coli SecB to the signal sequence region of a presecretory protein.Oligomeric complexes involved in translocation of proteins across the membrane of the endoplasmic reticulum.Interactions of ribosome nascent chain complexes of the chloroplast-encoded D1 thylakoid membrane protein with cpSRP54.Archaeal protein translocation crossing membranes in the third domain of life.Physiological basis for conservation of the signal recognition particle targeting pathway in Escherichia coli.Co-translational targeting and translocation of the amino terminus of opsin across the endoplasmic membrane requires GTP but not ATP.Signal recognition particle (SRP), a ubiquitous initiator of protein translocation.A chloroplast homologue of the signal recognition particle subunit SRP54 is involved in the posttranslational integration of a protein into thylakoid membranes.Signal sequence recognition and targeting of ribosomes to the endoplasmic reticulum by the signal recognition particle do not require GTP.DNA-strand exchange promoted by RecA protein in the absence of ATP: implications for the mechanism of energy transduction in protein-promoted nucleic acid transactions.The targeting pathway of Escherichia coli presecretory and integral membrane proteins is specified by the hydrophobicity of the targeting signalGenetic and biochemical analysis of the fission yeast ribonucleoprotein particle containing a homolog of Srp54p.Structure, function, and regulation of free and membrane-bound ribosomes: the view from their substrates and products.Molecular mechanism of signal sequence orientation in the endoplasmic reticulum.SRP meets the ribosome.Conformational changes in the GTPase modules of the signal reception particle and its receptor drive initiation of protein translocationVersatility of the endoplasmic reticulum protein folding factory.Identification of a novel stage of ribosome/nascent chain association with the endoplasmic reticulum membrane.Homoiterons and expansion in ribosomal RNAs
P2860
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P2860
GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation
description
1993 nî lūn-bûn
@nan
1993 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
GTP binding and hydrolysis by ...... ation of protein translocation
@ast
GTP binding and hydrolysis by ...... ation of protein translocation
@en
GTP binding and hydrolysis by ...... ation of protein translocation
@en-gb
GTP binding and hydrolysis by ...... ation of protein translocation
@nl
type
label
GTP binding and hydrolysis by ...... ation of protein translocation
@ast
GTP binding and hydrolysis by ...... ation of protein translocation
@en
GTP binding and hydrolysis by ...... ation of protein translocation
@en-gb
GTP binding and hydrolysis by ...... ation of protein translocation
@nl
prefLabel
GTP binding and hydrolysis by ...... ation of protein translocation
@ast
GTP binding and hydrolysis by ...... ation of protein translocation
@en
GTP binding and hydrolysis by ...... ation of protein translocation
@en-gb
GTP binding and hydrolysis by ...... ation of protein translocation
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P2093
P356
P1433
P1476
GTP binding and hydrolysis by ...... ation of protein translocation
@en
P2093
P2888
P356
10.1038/366351A0
P407
P577
1993-11-25T00:00:00Z
P5875
P6179
1029127639