A gene located at 72A in Drosophila melanogaster encodes a novel zinc-finger protein that interacts with protein kinase CK2

2001 ◽  
pp. 99-105
Author(s):  
Madhavi Kalive ◽  
Regina L. Trott ◽  
Ashok P. Bidwai
Keyword(s):  
Drosophila Melanogaster ◽  
Protein Kinase ◽  
Zinc Finger ◽  
Protein Kinase Ck2 ◽  
Zinc Finger Protein ◽  
Finger Protein ◽  
Kinase Ck2

The enhancer-blocking suppressor of Hairy-wing zinc finger protein of Drosophila melanogaster alters DNA structure

1994 ◽  
Vol 14 (9) ◽  
pp. 5645-5652
Author(s):  
B Shen ◽  
J Kim ◽  
D Dorsett
Keyword(s):  
Drosophila Melanogaster ◽  
Zinc Finger ◽  
Zinc Finger Protein ◽  
Dna Structure ◽  
Protein Domain ◽  
Transcription Activator ◽  
Long Distance ◽  
Dna Flexibility ◽  
Finger Protein ◽  
Enhancer Blocking

Insertion of the gypsy retrotransposon of Drosophila melanogaster into a gene control region can repress gene expression. The zinc finger protein (SUHW) encoded by the suppressor of Hairy-wing [su(Hw)] gene binds to gypsy and prevents gene enhancers from activating transcription. SUHW blocks an enhancer only when positioned between the enhancer and promoter. Although position dependent, SUHW enhancer blocking is distance independent. These properties indicate that SUHW does not interact with the transcription activator proteins that bind to enhancers. To explore if DNA distortions are involved in enhancer blocking, the ability of SUHW to alter DNA structure was examined in gel mobility assays. Indeed, SUHW induces an unusual change in the structure of the binding-site DNA. The change is not a directed DNA bend but correlates with loss of sequence-directed bends in the unbound DNA. The DNA distortion requires a SUHW protein domain not required for DNA binding, and mutant proteins that fail to alter DNA structure also fail to eliminate the sequence-directed bends. These results suggest that SUHW increases DNA flexibility. The DNA distortion is not sufficient to block enhancers, and therefore it is suggested that increased DNA flexibility may help SUHW interact and interfere with proteins that support long-distance enhancer-promoter interactions.

Two homologous zinc finger genes identified by multicopy suppression in a SNF1 protein kinase mutant of Saccharomyces cerevisiae

1993 ◽  
Vol 13 (7) ◽  
pp. 3872-3881
Author(s):  
F Estruch ◽  
M Carlson
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Kinase ◽  
Zinc Finger ◽  
Zinc Finger Protein ◽  
Wilms Tumor ◽  
Temperature Sensitive ◽  
Carbon Utilization ◽  
Functional Roles ◽  
Multicopy Suppressor ◽  
Finger Protein

The MSN2 gene was selected as a multicopy suppressor in a temperature-sensitive SNF1 protein kinase mutant of Saccharomyces cerevisiae. MSN2 encodes a Cys2His2 zinc finger protein related to the yeast MIG1 repressor and to mammalian early growth response and Wilms' tumor zinc finger proteins. Deletion of MSN2 caused no phenotype. A second similar zinc finger gene, MSN4, was isolated, and deletion of both genes caused phenotypic defects related to carbon utilization. Overexpression of the zinc finger regions was deleterious to growth. LexA-MSN2 and LexA-MSN4 fusion proteins functioned as strong transcriptional activators when bound to DNA. Functional roles of this zinc finger protein family are discussed.

scholarly journals Two homologous zinc finger genes identified by multicopy suppression in a SNF1 protein kinase mutant of Saccharomyces cerevisiae.

1993 ◽  
Vol 13 (7) ◽  
pp. 3872-3881 ◽  
Author(s):  
F Estruch ◽  
M Carlson
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Kinase ◽  
Zinc Finger ◽  
Zinc Finger Protein ◽  
Wilms Tumor ◽  
Temperature Sensitive ◽  
Carbon Utilization ◽  
Functional Roles ◽  
Multicopy Suppressor ◽  
Finger Protein

The MSN2 gene was selected as a multicopy suppressor in a temperature-sensitive SNF1 protein kinase mutant of Saccharomyces cerevisiae. MSN2 encodes a Cys2His2 zinc finger protein related to the yeast MIG1 repressor and to mammalian early growth response and Wilms' tumor zinc finger proteins. Deletion of MSN2 caused no phenotype. A second similar zinc finger gene, MSN4, was isolated, and deletion of both genes caused phenotypic defects related to carbon utilization. Overexpression of the zinc finger regions was deleterious to growth. LexA-MSN2 and LexA-MSN4 fusion proteins functioned as strong transcriptional activators when bound to DNA. Functional roles of this zinc finger protein family are discussed.

scholarly journals Nuclear localization of the C2H2 zinc finger protein Msn2p is regulated by stress and protein kinase A activity

1998 ◽  
Vol 12 (4) ◽  
pp. 586-597 ◽  
Author(s):  
W. Gorner ◽  
E. Durchschlag ◽  
M. T. Martinez-Pastor ◽  
F. Estruch ◽  
G. Ammerer ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Zinc Finger ◽  
Nuclear Localization ◽  
Zinc Finger Protein ◽  
C2h2 Zinc Finger ◽  
Finger Protein ◽  
C2h2 Zinc Finger Protein ◽  
Kinase A

Assembly of protein kinase CK2: investigation of complex formation between catalytic and regulatory subunits using a zinc-finger-deficient mutant of CK2β

2001 ◽  
Vol 358 (1) ◽  
pp. 87-94 ◽  
Author(s):  
David A. CANTON ◽  
Cunjie ZHANG ◽  
David W. LITCHFIELD
Keyword(s):  
Protein Kinase ◽  
Zinc Finger ◽  
Protein Kinase Ck2 ◽  
Deficient Mutant ◽  
Binding Assays ◽  
Catalytic Subunits ◽  
Regulatory Subunits ◽  
Regulatory Ck2β Subunit ◽  
Kinase Ck2

Protein kinase CK2 is a tetrameric enzyme comprised of two regulatory subunits (CK2β) and two catalytic subunits (CK2α and/or CK2α′). The crystal structure of dimeric CK2β demonstrated that a zinc finger mediates CK2β dimerization, therefore we constructed a mutant in which cysteine residues 109 and 114 were mutated to serine. Our objectives were to examine the effects of disrupting the zinc finger of the regulatory CK2β subunit on CK2 tetramer assembly. Examination of this zinc-finger-deficient mutant of CK2β using a yeast two-hybrid assay demonstrates that the mutant fails to form CK2β homodimers. In order to extend these studies, we co-transfected COS-7 cells with epitope-tagged constructs and performed co-immunoprecipitation assays. The results from these studies demonstrate that the mutant fails to form CK2β homodimers and fails to interact with catalytic CK2 subunits. Furthermore, we demonstrate that the mutant CK2β is not appreciably phosphorylated in cells. Using in vitro binding assays, we demonstrated that the mutant CK2β protein fails to interact with glutathione S-transferase–CK2α′. Finally, we demonstrate that the mutant is translated at an equivalent rate to wild-type CK2β, but is degraded much more rapidly. Overall, our results are consistent with the model that β–β dimerization precedes incorporation of catalytic subunits into tetrameric CK2 complexes, and that β–β dimerization is a prerequisite for the stable incorporation of catalytic subunits into CK2 complexes.

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