scholarly journals Single-strand binding protein enhances invasion of a PNA strand to double-stranded DNA

2008 ◽  
Vol 52 (1) ◽  
pp. 141-142 ◽  
Author(s):  
T. Ishizuka ◽  
M. Komiyama
Keyword(s):  
Binding Protein ◽  
Single Strand ◽  
Double Stranded Dna

scholarly journals Multiple single-stranded cis elements are associated with activated chromatin of the human c-myc gene in vivo.

1996 ◽  
Vol 16 (6) ◽  
pp. 2656-2669 ◽  
Author(s):  
G A Michelotti ◽  
E F Michelotti ◽  
A Pullner ◽  
R C Duncan ◽  
D Eick ◽  
...  
Keyword(s):  
Binding Protein ◽  
Single Strand ◽  
Upstream Sequence ◽  
Cis Elements ◽  
Sequence Element ◽  
S1 Nuclease ◽  
Heterogeneous Nuclear Ribonucleoprotein ◽  
Myc Gene ◽  
Nuclear Ribonucleoprotein

Transcription activation and repression of eukaryotic genes are associated with conformational and topological changes of the DNA and chromatin, altering the spectrum of proteins associated with an active gene. Segments of the human c-myc gene possessing non-B structure in vivo located with enzymatic and chemical probes. Sites hypertensive to cleavage with single-strand-specific S1 nuclease or the single-strand-selective agent potassium permanganate included the major promoters P1 and P2 as well as the far upstream sequence element (FUSE) and CT elements, which bind, respectively, the single-strand-specific factors FUSE-binding protein and heterogeneous nuclear ribonucleoprotein K in vitro. Active and inactive c-myc genes yielded different patterns of S1 nuclease and permanganate sensitivity, indicating alternative chromatin configurations of active and silent genes. The melting of specific cis elements of active c-myc genes in vivo suggested that transcriptionally associated torsional strain might assist strand separation and facilitate factor binding. Therefore, the interaction of FUSE-binding protein and heterogeneous nuclear ribonucleoprotein K with supercoiled DNA was studied. Remarkably, both proteins recognize their respective elements torsionally strained but not as liner duplexes. Single-strand- or supercoil-dependent gene regulatory proteins may directly link alterations in DNA conformation and topology with changes in gene expression.

A possible interaction of single-strand binding protein and RecA protein during post-ultraviolet DNA synthesis

Biochimie ◽  
1991 ◽  
Vol 73 (4) ◽  
pp. 515-517 ◽  
Author(s):  
Zˇ. Trovcˇević ◽  
M. Petranović ◽  
K. Brcˇić-Kostić ◽  
D. Petranović ◽  
N. Lersˇ ◽  
...  
Keyword(s):  
Dna Synthesis ◽  
Binding Protein ◽  
Reca Protein ◽  
Single Strand

scholarly journals The mechanism of Single strand binding protein–RecG binding: Implications for SSB interactome function

2020 ◽  
Vol 29 (5) ◽  
pp. 1211-1227 ◽  
Author(s):  
Wenfei Ding ◽  
Hui Yin Tan ◽  
Jia Xiang Zhang ◽  
Luke A. Wilczek ◽  
Karin R. Hsieh ◽  
...  
Keyword(s):  
Binding Protein ◽  
Single Strand

scholarly journals The Saccharomyces telomere-binding protein Cdc13p interacts with both the catalytic subunit of DNA polymerase α and the telomerase-associated Est1 protein

2000 ◽  
Vol 14 (14) ◽  
pp. 1777-1788 ◽  
Author(s):  
Haiyan Qi ◽  
Virginia A. Zakian
Keyword(s):  
Dna Polymerase ◽  
Binding Protein ◽  
Point Mutations ◽  
Single Strand ◽  
Catalytic Subunit ◽  
Full Length ◽  
Temperature Sensitive ◽  
Dna Polymerase Α ◽  
Telomere Binding Protein

Saccharomyces telomeres consist of ∼350 bp of C1-3A/TG1-3 DNA. Most of this ∼350 bp is replicated by standard, semiconservative DNA replication. After conventional replication, the C1-3A strand is degraded to generate a long single strand TG1-3 tail that can serve as a substrate for telomerase. Cdc13p is a single strand TG1-3DNA-binding protein that localizes to telomeres in vivo. Genetic data suggest that the Cdc13p has multiple roles in telomere replication. We used two hybrid analysis to demonstrate that Cdc13p interacted with both the catalytic subunit of DNA polymerase α, Pol1p, and the telomerase RNA-associated protein, Est1p. The association of these proteins was confirmed by biochemical analysis using full-length or nearly full-length proteins. Point mutations in either CDC13 orPOL1 that reduced the Cdc13p–Pol1p interaction resulted in telomerase mediated telomere lengthening. Over–expression of the carboxyl terminus of Est1p partially suppressed the temperature sensitive lethality of a cdc13-1 strain. We propose that Cdc13p's interaction with Est1p promotes TG1-3 strand lengthening by telomerase and its interaction with Pol1p promotes C1-3A strand resynthesis by DNA polymerase α.

Conformational Change in the Herpes Simplex Single-Strand Binding Protein Induced by DNA

2001 ◽  
Vol 288 (1) ◽  
pp. 184-190 ◽  
Author(s):  
Kathleen C. Dudas ◽  
Sarah K. Scouten ◽  
William T. Ruyechan
Keyword(s):  
Herpes Simplex ◽  
Conformational Change ◽  
Binding Protein ◽  
Single Strand
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