CPY Document
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or a tr as ac tio n. A l p rim ar y so ur ce s ar e no t e qu al in v al ue . T yp ic al y, a ca de m ic h is to ria ns tu rn to s uc h p r i t e d r e c o r d s f o r th e st ar tin g po in t o f th ei r st ud y, M os t p le nt if ul a re g ov er ne nt a nd c hu rc h re co rd s, bu t n ew sp ap er s, d ia re s, p ri va te le tte rs , c or po ra te r ec or ds o f un iv er si tie s, or b us in es se s, li te ra ry te xt s, a nd m in ut es o f m ee tin gs a re o nl y a fe w o f t he so ur ce s th at c an b e g i t o u n c o v e r in fo nn at io n. O ff ci al r ec or ds o f th is s or t
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Characterization of the Hansenula polymorpha CPY gene encoding carboxypeptidase
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متن کاملCharacterization of the Hansenula polymorpha CPY gene encoding carboxypeptidase Y.
We have isolated the Hansenula polymorpha CPY gene encoding carboxypeptidase Y (Hp-CPY). The deduced amino acid sequence revealed that Hp-CPY consists of 541 amino acids and has a calculated Mr of 60,793. The protein is highly similar to Saccharomyces cerevisiae CPY (61.8% identity). At the N-terminus of Hp-CPY signals for the entry into the secretory pathway and subsequent sorting to the vacuo...
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We have identified a new pathway of ER-associated degradation in Saccharomyces cerevisiae that functions separately from the HRD/DER pathway comprised of Hrd1p, Hrd3p, Der1p, and Ubc7p. This pathway, termed Hrd1p independent-proteolysis (HIP), is capable of recognizing and degrading both lumenal (CPY* and PrA*), and integral membrane proteins (Sec61-2p) that misfold in the ER. CPY* overexpressi...
متن کاملER-golgi traffic is a prerequisite for efficient ER degradation.
Protein quality control is an essential function of the endoplasmic reticulum. Misfolded proteins unable to acquire their native conformation are retained in the endoplasmic reticulum, retro-translocated back into the cytosol, and degraded via the ubiquitin-proteasome system. We show that efficient degradation of soluble malfolded proteins in yeast requires a fully competent early secretory pat...
متن کاملRetention of a co-translational translocated mutant protein of carboxypeptidase Y of Saccharomyces cerevisiae in endoplasmic reticulum.
Co-translational translocation of Saccharomyces cerevisiae vacuolar glycoprotein carboxypeptidase Y (CpY) was highly efficient when studied with an in vivo and in vitro homologous system, comparison of limited proteolytic cleavage of immunoprecipitated translational products of CpY and subcellular localisation of a mutant CpY. The efficient segregation of CpY mRNA in highly purified fractions o...
متن کاملGene dosage-dependent secretion of yeast vacuolar carboxypeptidase Y
The structural gene for yeast vacuolar carboxypeptidase Y (PRC1) has been cloned by complementation of the prc1-1 mutation. As much as an eightfold elevation in the level of carboxypeptidase Y (CPY) results when a multiple-copy plasmid containing the PRC1 gene is introduced into yeast. Unlike the situation with a single copy of PRC1 in which newly synthesized CPY is efficiently localized to the...
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