PMID- 2201897
OWN - NLM
STAT- MEDLINE
DCOM- 19900926
LR  - 20210526
IS  - 0270-7306 (Print)
IS  - 1098-5549 (Electronic)
IS  - 0270-7306 (Linking)
VI  - 10
IP  - 9
DP  - 1990 Sep
TI  - Phosphorylated forms of GAL4 are correlated with ability to activate 
      transcription.
PG  - 4623-9
AB  - GAL4I, GAL4II, and GAL4III are three forms of the yeast transcriptional activator 
      protein that are readily distinguished on the basis of electrophoretic mobility 
      during sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Phosphorylation 
      accounts for the reduced mobility of the slowest-migrating form, GAL4III, which 
      is found to be closely associated with high-level GAL/MEL gene expression (L. 
      Mylin, P. Bhat, and J. Hopper, Genes Dev. 3:1157-1165, 1989). Here we show that 
      GAL4II, like GAL4III, can be converted to GAL4I by phosphatase treatment, 
      suggesting that in vivo GAL4II is derived from GAL4I by phosphorylation. We found 
      that cells which overproduced GAL4 under conditions in which it drove moderate to 
      low levels of GAL/MEL gene expression showed only forms GAL4I and GAL4II. To 
      distinguish which forms of GAL4 (GAL4I, GAL4II, or both) might be responsible for 
      transcription activation in the absence of GAL4III, we performed immunoblot 
      analysis on UASgal-binding-competent GAL4 proteins from four gal4 missense 
      mutants selected for their inability to activate transcription (M. Johnston and 
      J. Dover, Proc. Natl. Acad. Sci. USA 84:2401-2405, 1987; Genetics 120;63-74, 
      1988). The three mutants with no detectable GAL1 expression did not appear to 
      form GAL4II or GAL4III, but revertants in which GAL4-dependent transcription was 
      restored did display GAL4II- or GAL4III-like electrophoretic species. Detection 
      of GAL4II in a UASgal-binding mutant suggests that neither UASgal binding nor 
      GAL/MEL gene activation is required for the formation of GAL4II. Overall, our 
      results imply that GAL4I may be inactive in transcriptional activation, whereas 
      GAL4II appears to be active. In light of this work, we hypothesize that 
      phosphorylation of GAL4I makes it competent to activate transcription.
FAU - Mylin, L M
AU  - Mylin LM
AD  - Department of Biological Chemistry, Milton S. Hershey Medical Center, 
      Pennsylvania State University, Hershey 17033.
FAU - Johnston, M
AU  - Johnston M
FAU - Hopper, J E
AU  - Hopper JE
LA  - eng
GR  - R01 GM032540/GM/NIGMS NIH HHS/United States
GR  - GM27925/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Mol Cell Biol
JT  - Molecular and cellular biology
JID - 8109087
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Fungal Proteins)
RN  - 0 (GAL4 protein, S cerevisiae)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - 0 (Transcription Factors)
SB  - IM
MH  - Alleles
MH  - DNA-Binding Proteins
MH  - Fungal Proteins/*genetics/isolation & purification/metabolism
MH  - *Gene Expression Regulation, Fungal
MH  - Genetic Variation
MH  - Genotype
MH  - Mutation
MH  - Phosphorylation
MH  - Saccharomyces cerevisiae/*genetics/metabolism
MH  - *Saccharomyces cerevisiae Proteins
MH  - Transcription Factors/*genetics
MH  - *Transcription, Genetic
MH  - Transcriptional Activation
PMC - PMC361051
EDAT- 1990/09/01 00:00
MHDA- 1990/09/01 00:01
PMCR- 1990/09/01
CRDT- 1990/09/01 00:00
PHST- 1990/09/01 00:00 [pubmed]
PHST- 1990/09/01 00:01 [medline]
PHST- 1990/09/01 00:00 [entrez]
PHST- 1990/09/01 00:00 [pmc-release]
AID - 10.1128/mcb.10.9.4623-4629.1990 [doi]
PST - ppublish
SO  - Mol Cell Biol. 1990 Sep;10(9):4623-9. doi: 10.1128/mcb.10.9.4623-4629.1990.