scholarly journals Structures of apo- and ssDNA-bound YdbC from Lactococcus lactis uncover the function of protein domain family DUF2128 and expand the single-stranded DNA-binding domain proteome

2013 ◽  
Vol 41 (4) ◽  
pp. 2756-2768 ◽  
Author(s):  
Paolo Rossi ◽  
Christopher M. Barbieri ◽  
James M. Aramini ◽  
Elisabetta Bini ◽  
Hsiau-Wei Lee ◽  
...  
Keyword(s):  
Dna Binding ◽  
Lactococcus Lactis ◽  
Binding Domain ◽  
Protein Domain ◽  
Dna Binding Domain ◽  
Domain Family ◽  
Single Stranded Dna ◽  
Protein Domain Family

scholarly journals Properties of the DNA-binding domain of the simian virus 40 large T antigen.

1989 ◽  
Vol 9 (12) ◽  
pp. 5525-5536 ◽  
Author(s):  
D McVey ◽  
M Strauss ◽  
Y Gluzman
Keyword(s):  
Amino Acids ◽  
Dna Binding ◽  
Dna Analysis ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
T Antigen ◽  
Binding Domain ◽  
Protein Domain ◽  
Dna Binding Domain ◽  
Single Stranded Dna

T antigen (Tag) from simian virus 40 binds specifically to two distinct sites in the viral origin of replication and to single-stranded DNA. Analysis of the protein domain responsible for these activities revealed the following. (i) The C-terminal boundary of the origin-specific and single-strand-specific DNA-binding domain is at or near amino acid 246; furthermore, the maximum of these DNA-binding activities coincides with a narrow C-terminal boundary, spanning 4 amino acids (246 to 249) and declines sharply in proteins with C termini which differ by a few (4 to 10) amino acids; (ii) a polypeptide spanning residues 132 to 246 of Tag is an independent domain responsible for origin-specific DNA binding and presumably for single-stranded DNA binding; and (iii) a comparison of identical N-terminal fragments of Tag purified from mammalian and bacterial cells revealed differential specificity and levels of activity between the two sources of protein. A role for posttranslational modification (phosphorylation) in controlling the DNA-binding activity of Tag is discussed.

Properties of the DNA-binding domain of the simian virus 40 large T antigen

1989 ◽  
Vol 9 (12) ◽  
pp. 5525-5536
Author(s):  
D McVey ◽  
M Strauss ◽  
Y Gluzman
Keyword(s):  
Amino Acids ◽  
Dna Binding ◽  
Dna Analysis ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
T Antigen ◽  
Binding Domain ◽  
Protein Domain ◽  
Dna Binding Domain ◽  
Single Stranded Dna

T antigen (Tag) from simian virus 40 binds specifically to two distinct sites in the viral origin of replication and to single-stranded DNA. Analysis of the protein domain responsible for these activities revealed the following. (i) The C-terminal boundary of the origin-specific and single-strand-specific DNA-binding domain is at or near amino acid 246; furthermore, the maximum of these DNA-binding activities coincides with a narrow C-terminal boundary, spanning 4 amino acids (246 to 249) and declines sharply in proteins with C termini which differ by a few (4 to 10) amino acids; (ii) a polypeptide spanning residues 132 to 246 of Tag is an independent domain responsible for origin-specific DNA binding and presumably for single-stranded DNA binding; and (iii) a comparison of identical N-terminal fragments of Tag purified from mammalian and bacterial cells revealed differential specificity and levels of activity between the two sources of protein. A role for posttranslational modification (phosphorylation) in controlling the DNA-binding activity of Tag is discussed.

scholarly journals The RPA32 Subunit of Human Replication Protein A Contains a Single-stranded DNA-binding Domain

1998 ◽  
Vol 273 (7) ◽  
pp. 3932-3936 ◽  
Author(s):  
Elena Bochkareva ◽  
Lori Frappier ◽  
Aled M. Edwards ◽  
Alexey Bochkarev
Keyword(s):  
Dna Binding ◽  
Protein A ◽  
Replication Protein A ◽  
Binding Domain ◽  
Replication Protein ◽  
Dna Binding Domain ◽  
Single Stranded Dna

scholarly journals Nonadditivity in the Recognition of Single-Stranded DNA by theSchizosaccharomyces pombeProtection of Telomeres 1 DNA-Binding Domain, Pot1-DBD

Biochemistry ◽  
2009 ◽  
Vol 48 (29) ◽  
pp. 6864-6875 ◽  
Author(s):  
Johnny E. Croy ◽  
Sarah E. Altschuler ◽  
Nicole E. Grimm ◽  
Deborah S. Wuttke
Keyword(s):  
Dna Binding ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Single Stranded Dna

scholarly journals Characterization of the DNA-Binding Domain of the Avian Y-Box Protein, chkYB-2, and Mutational Analysis of Its Single-Strand Binding Motif in the Rous Sarcoma Virus Enhancer

1998 ◽  
Vol 72 (2) ◽  
pp. 900-909 ◽  
Author(s):  
Ashok Nambiar ◽  
S. K. Swamynathan ◽  
Jagannadha C. Kandala ◽  
Ramareddy V. Guntaka
Keyword(s):  
Dna Binding ◽  
Rous Sarcoma Virus ◽  
Mutational Analysis ◽  
Binding Domain ◽  
Single Strand ◽  
Dna Binding Domain ◽  
Single Stranded Dna ◽  
High Affinity ◽  
Rous Sarcoma ◽  
Sarcoma Virus

ABSTRACT chkYB-2 is a sequence-specific, single-stranded DNA binding chicken Y-box protein that promotes Rous sarcoma virus long terminal repeat (RSV LTR)-driven transcription in avian fibroblasts. The DNA-binding domain of chkYB-2 has been mapped by characterizing the DNA binding properties of purified recombinant chkYB-2 mutant polypeptides. The data indicate that the invariant cold shock domain (CSD) is necessary but not sufficient for association with DNA and suggest that another conserved region, adjacent to the carboxyl boundary of the CSD, plays a role in high-affinity DNA binding. chkYB-2 binds to a tandem repeat of the 5′-GTACCACC-3′ motif on the RSV LTR. Mutational analysis of this recognition sequence revealed the requirement of an essentially unaltered template for both high-affinity binding by chkYB-2 as well as maximal transcriptional activity of the RSV LTR in vivo. The single-stranded DNA binding activity of chkYB-2 is augmented by Mg2+. The possible significance of this finding for transactivation by a single-strand DNA binding protein is discussed.

Sign in / Sign up

Export Citation Format

Share Document