Secretion in yeast: translocation and glycosylation of prepro-alpha-factor in vitro can occur via an ATP-dependent post-translational mechanism.
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The refolding activity of the yeast heat shock proteins Ssa1 and Ssa2 defines their role in protein translocationBiP and Sec63p are required for both co- and posttranslational protein translocation into the yeast endoplasmic reticulum.Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeastTwo alternative binding mechanisms connect the protein translocation Sec71-Sec72 complex with heat shock proteins.SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli.Phosphatidylinositol-glycan (PI-G)-anchored membrane proteins: requirement of ATP and GTP for translation-independent COOH-terminal processingAzide-resistant mutants of Escherichia coli alter the SecA protein, an azide-sensitive component of the protein export machinery.ProOmpA contains secondary and tertiary structure prior to translocation and is shielded from aggregation by association with SecB proteinIntracellular traffic of newly synthesized proteins. Current understanding and future prospectsOn the translocation of proteins across membranes.Protein import into chloroplasts requires a chloroplast ATPaseSoluble factors stimulating secretory protein translocation in bacteria and yeast can substitute for each other.A yeast mutant defective at an early stage in import of secretory protein precursors into the endoplasmic reticulum.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.Yeast carboxypeptidase Y can be translocated and glycosylated without its amino-terminal signal sequence.Formation of a functional ribosome-membrane junction during translocation requires the participation of a GTP-binding protein.Protein translocation across the yeast microsomal membrane is stimulated by a soluble factorDithiothreitol and the translocation of preprolactin across mammalian endoplasmic reticulumTranslocation in yeast and mammalian cells: not all signal sequences are functionally equivalent.Translocation of acyl-CoA oxidase into peroxisomes requires ATP hydrolysis but not a membrane potentialFull-length prepro-alpha-factor can be translocated across the mammalian microsomal membrane only if translation has not terminated.Prepro-carboxypeptidase Y and a truncated form of pre-invertase, but not full-length pre-invertase, can be posttranslationally translocated across microsomal vesicle membranes from Saccharomyces cerevisiae.Integration of membrane proteins into the endoplasmic reticulum requires GTPReconstitution of protein transport from the endoplasmic reticulum to the Golgi complex in yeast: the acceptor Golgi compartment is defective in the sec23 mutant.SEC62 encodes a putative membrane protein required for protein translocation into the yeast endoplasmic reticulum.Saccharomyces cerevisiae and Schizosaccharomyces pombe contain a homologue to the 54-kD subunit of the signal recognition particle that in S. cerevisiae is essential for growthMutants in three novel complementation groups inhibit membrane protein insertion into and soluble protein translocation across the endoplasmic reticulum membrane of Saccharomyces cerevisiaeProtein translocation across the rough endoplasmic reticulum.Mutations in the signal sequence of prepro-alpha-factor inhibit both translocation into the endoplasmic reticulum and processing by signal peptidase in yeast cells.The N-terminal (pre-S2) domain of a hepatitis B virus surface glycoprotein is translocated across membranes by downstream signal sequences.Signal processing, glycosylation, and secretion of mutant hemagglutinins of a human influenza virus by Saccharomyces cerevisiae.Amino-terminal sequence, synthesis, and membrane insertion of glycoprotein B of herpes simplex virus type 1.The yeast acid phosphatase can enter the secretory pathway without its N-terminal signal sequence.Specific molecular chaperone interactions and an ATP-dependent conformational change are required during posttranslational protein translocation into the yeast ER.Insertion of proteins into bacterial membranes: mechanism, characteristics, and comparisons with the eucaryotic process.Protein secretion in Bacillus species.Genetic interactions between KAR2 and SEC63, encoding eukaryotic homologues of DnaK and DnaJ in the endoplasmic reticulum.Membrane integration of in vitro-translated gap junctional proteins: co- and post-translational mechanisms.Protein O-mannosyltransferases associate with the translocon to modify translocating polypeptide chains.Nascent secretory polypeptides synthesized on Escherichia coli ribosomes are not translocated across mammalian endoplasmic reticulum.
P2860
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P2860
Secretion in yeast: translocation and glycosylation of prepro-alpha-factor in vitro can occur via an ATP-dependent post-translational mechanism.
description
1986 nî lūn-bûn
@nan
1986年の論文
@ja
1986年論文
@yue
1986年論文
@zh-hant
1986年論文
@zh-hk
1986年論文
@zh-mo
1986年論文
@zh-tw
1986年论文
@wuu
1986年论文
@zh
1986年论文
@zh-cn
name
Secretion in yeast: translocat ...... post-translational mechanism.
@en
Secretion in yeast: translocat ...... post-translational mechanism.
@nl
type
label
Secretion in yeast: translocat ...... post-translational mechanism.
@en
Secretion in yeast: translocat ...... post-translational mechanism.
@nl
prefLabel
Secretion in yeast: translocat ...... post-translational mechanism.
@en
Secretion in yeast: translocat ...... post-translational mechanism.
@nl
P2860
P1433
P1476
Secretion in yeast: translocat ...... t post-translational mechanism
@en
P2093
J A Rothblatt
P2860
P304
P356
10.1002/J.1460-2075.1986.TB04318.X
P407
P577
1986-05-01T00:00:00Z