scholarly journals High salt- and SDS-stable DNA binding protein complexes with ATPase and protein kinase activity retained in chromatin-depleted nuclei

1995 ◽  
Vol 23 (8) ◽  
pp. 1359-1366 ◽  
Author(s):  
Benediktas Juodka ◽  
Eberhard Spiess ◽  
Antonella Angiolillo ◽  
Gaby Joswig ◽  
Karsten Rothbarth ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Dna Binding ◽  
Kinase Activity ◽  
Protein Complexes ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
High Salt ◽  
Protein Kinase Activity

Heme: emergent roles of heme in signal transduction, functional regulation and as catalytic centres

2019 ◽  
Vol 48 (24) ◽  
pp. 5624-5657 ◽  
Author(s):  
Toru Shimizu ◽  
Alzbeta Lengalova ◽  
Václav Martínek ◽  
Markéta Martínková
Keyword(s):  
Signal Transduction ◽  
Protein Kinase ◽  
Dna Binding ◽  
Heme Proteins ◽  
Molecular Mechanisms ◽  
Kinase Activity ◽  
Bond Formation ◽  
Dna Binding Protein ◽  
Protein Kinase Activity ◽  
Functional Regulation

Molecular mechanisms of unprecedented functions of exchangeable/labile heme and heme proteins including transcription, DNA binding, protein kinase activity, K+ channel functions, cis–trans isomerization, N–N bond formation, and other functions are described.

scholarly journals The major histocompatibility complex class II promoter-binding protein RFX (NF-X) is a methylated DNA-binding protein.

1993 ◽  
Vol 13 (11) ◽  
pp. 6810-6818 ◽  
Author(s):  
X Y Zhang ◽  
N Jabrane-Ferrat ◽  
C K Asiedu ◽  
S Samac ◽  
B M Peterlin ◽  
...  
Keyword(s):  
Dna Methylation ◽  
Dna Binding ◽  
Dna Sequences ◽  
Protein Complexes ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Class Ii ◽  
Major Histocompatibility ◽  
Methylated Dna ◽  
Mammalian Protein

A mammalian protein called RFX or NF-X binds to the X box (or X1 box) in the promoters of a number of major histocompatibility (MHC) class II genes. In this study, RFX was shown to have the same DNA-binding specificity as methylated DNA-binding protein (MDBP), and its own cDNA was found to contain a binding site for MDBP in the leader region. MDBP is a ubiquitous mammalian protein that binds to certain DNA sequences preferentially when they are CpG methylated and to other related sequences, like the X box, irrespective of DNA methylation. MDBP from HeLa and Raji cells formed DNA-protein complexes with X-box oligonucleotides that coelectrophoresed with those containing standard MDBP sites. Furthermore, MDBP and X-box oligonucleotides cross-competed for the formation of these DNA-protein complexes. DNA-protein complexes obtained with MDBP sites displayed the same partial supershifting with an antiserum directed to the N terminus of RFX seen for complexes containing an X-box oligonucleotide. Also, the in vitro-transcribed-translated product of a recombinant RFX cDNA bound specifically to MDBP ligands and displayed the DNA methylation-dependent binding of MDBP. RFX therefore contains MDBP activity and thereby also EF-C, EP, and MIF activities that are indistinguishable from MDBP and that bind to methylation-independent sites in the transcriptional enhancers of polyomavirus and hepatitis B virus and to an intron of c-myc.

Regulation of meiosis: From DNA binding protein to protein kinase

BioEssays ◽  
1989 ◽  
Vol 11 (1) ◽  
pp. 9-14 ◽  
Author(s):  
Maureen McLeod
Keyword(s):  
Protein Kinase ◽  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein

Identification of a protein kinase activity in rabbit reticulocytes that phosphorylates the mRNA cap binding protein

1988 ◽  
Vol 153 (1) ◽  
pp. 340-346 ◽  
Author(s):  
E. Lynne McMullin ◽  
David W. Haas ◽  
Richard D. Abramson ◽  
Robert E. Thach ◽  
William C. Merrick ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Kinase Activity ◽  
Binding Protein ◽  
Protein Kinase Activity ◽  
Rabbit Reticulocytes

scholarly journals Characterization of a Ku86 Variant Protein That Results in Altered DNA Binding and Diminished DNA-dependent Protein Kinase Activity

1996 ◽  
Vol 271 (24) ◽  
pp. 14098-14104 ◽  
Author(s):  
Zhiyong Han ◽  
Christine Johnston ◽  
Westley H. Reeves ◽  
Timothy Carter ◽  
James H. Wyche ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Dna Binding ◽  
Kinase Activity ◽  
Protein Kinase Activity ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
Variant Protein

scholarly journals Novel insight into the composition of human single-stranded DNA-binding protein 1 (hSSB1)-containing protein complexes

2016 ◽  
Vol 17 (1) ◽  
Author(s):  
Nicholas W. Ashton ◽  
Dorothy Loo ◽  
Nicolas Paquet ◽  
Kenneth J. O’Byrne ◽  
Derek J. Richard
Keyword(s):  
Dna Binding ◽  
Protein Complexes ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Single Stranded Dna ◽  
Insight Into

scholarly journals Synergistic release from glucose repression by mig1 and ssn mutations in Saccharomyces cerevisiae.

Genetics ◽  
1994 ◽  
Vol 137 (1) ◽  
pp. 49-54 ◽  
Author(s):  
L G Vallier ◽  
M Carlson
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Kinase ◽  
Dna Binding ◽  
Glucose Repression ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Yeast Saccharomyces Cerevisiae ◽  
Suc2 Promoter ◽  
Repressor Complex ◽  
Glucose Availability

Abstract In the yeast Saccharomyces cerevisiae, glucose repression of SUC2 transcription requires the SSN6-TUP1 repressor complex. It has been proposed that the DNA-binding protein MIG1 secures SSN6-TUP1 to the SUC2 promoter. Here we show that a mig1 deletion does not cause nearly as dramatic a loss of repression as ssn6: glucose-grown mig1 mutants display 20-fold lower SUC2 expression than ssn6 mutants. Thus, repression by SSN6-TUP1 is not mediated solely by MIG1, but also involves MIG1-independent mechanisms. We report that mig1 partially restores SUC2 expression in mutants lacking the SNF1 protein kinase and show that mig1 is allelic to ssn1, a mutation selected as a suppressor of snf1. Other SSN genes identified in this selection were therefore candidates for a role in repression of SUC2. We show that mig1 acts synergistically with ssn2 through ssn5, ssn7, and ssn8 to relieve glucose repression of SUC2 and to suppress the requirement for SNF1. These findings indicate that the SSN proteins contribute to repression of SUC2, and the pleiotropic phenotypes of the ssn mutants suggest global roles in repression. Finally, the regulated SUC2 expression observed in snf1 mig1 mutants indicates that signals regarding glucose availability can be transmitted independently of the SNF1 protein kinase.

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