Literature DB >> 7827405

Growth-related coordinate regulation of the early N-glycosylation genes in yeast.

M A Kukuruzinska1, K Lennon.   

Abstract

The Saccharomyces cerevisiae ALG7, ALG1 and ALG2 genes, whose products function early in the dolichol pathway of protein N-glycosylation, are essential for cell viability, and perturbation in their expression causes G1-specific cell cycle arrest. Here, we show that expression of the ALG7, ALG1 and ALG2 genes is coordinately regulated at the G0/G1 transition point in the yeast life cycle. Carbon starvation, which induces cells to exit from the G1 stage of the mitotic cycle into G0, resulted in a time-dependent decrease in the levels of the early ALG genes' mRNAs. Accordingly, addition of glucose, which stimulates the G0-arrested cells to resume proliferation, resulted in a rapid induction of their mRNAs. Cycloheximide alone also induced the early ALG transcripts, albeit to a much lower extent than glucose. Simultaneous addition of glucose and cycloheximide caused superinduction of these mRNAs, indicating that more than one control level was involved in their activation. Consistent with this, rapid degradation of ALG7, ALG1 and ALG2 mRNAs was completely abolished in the presence of cycloheximide. These data suggest that in yeast, the early N-glycosylation genes are regulated in a manner similar to that of the early growth-response genes.

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Year:  1994        PMID: 7827405     DOI: 10.1093/glycob/4.4.437

Source DB:  PubMed          Journal:  Glycobiology        ISSN: 0959-6658            Impact factor:   4.313


  8 in total

1.  Characterization of multiple transcripts of the hamster dolichol-P-dependent N-acetylglucosamine-1-P transferase suggests functionally complex expression.

Authors:  G T Huang; K Lennon; M A Kukuruzinska
Journal:  Mol Cell Biochem       Date:  1998-04       Impact factor: 3.396

2.  The dual role of mRNA half-lives in the expression of the yeast ALG7 gene.

Authors:  K Lennon; A Bird; Y F Chen; R Pretel; M A Kukuruzinska
Journal:  Mol Cell Biochem       Date:  1997-04       Impact factor: 3.396

3.  Heterologous secretory expression of β-glucosidase from Thermoascus aurantiacus in industrial Saccharomyces cerevisiae strains.

Authors:  Izat Smekenov; Marzhan Bakhtambayeva; Kudaybergen Bissenbayev; Murat Saparbayev; Sabira Taipakova; Amangeldy K Bissenbaev
Journal:  Braz J Microbiol       Date:  2019-11-28       Impact factor: 2.476

4.  Mapping N-linked glycosylation sites in the secretome and whole cells of Aspergillus niger using hydrazide chemistry and mass spectrometry.

Authors:  Lu Wang; Uma K Aryal; Ziyu Dai; Alisa C Mason; Matthew E Monroe; Zhi-Xin Tian; Jian-Ying Zhou; Dian Su; Karl K Weitz; Tao Liu; David G Camp; Richard D Smith; Scott E Baker; Wei-Jun Qian
Journal:  J Proteome Res       Date:  2011-12-02       Impact factor: 4.466

5.  Regulation of UDP-N-acetylglucosamine:dolichyl-phosphate N-acetylglucosamine-1-phosphate transferase by retinoic acid in P19 cells.

Authors:  J D Meissner; A Naumann; W H Mueller; R J Scheibe
Journal:  Biochem J       Date:  1999-03-01       Impact factor: 3.857

6.  Overexpression of a gene that encodes the first enzyme in the biosynthesis of asparagine-linked glycans makes plants resistant to tunicamycin and obviates the tunicamycin-induced unfolded protein response.

Authors:  N Koizumi; T Ujino; H Sano; M J Chrispeels
Journal:  Plant Physiol       Date:  1999-10       Impact factor: 8.340

7.  O-GlcNAc-specific antibody CTD110.6 cross-reacts with N-GlcNAc2-modified proteins induced under glucose deprivation.

Authors:  Takahiro Isono
Journal:  PLoS One       Date:  2011-04-19       Impact factor: 3.240

Review 8.  Protein N-glycosylation in oral cancer: dysregulated cellular networks among DPAGT1, E-cadherin adhesion and canonical Wnt signaling.

Authors:  Xaralabos Varelas; Meghan P Bouchie; Maria A Kukuruzinska
Journal:  Glycobiology       Date:  2014-04-17       Impact factor: 4.313

  8 in total

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