Single-Stranded DNA Binding Proteins Involved in Genome Maintenance

A sequence-specific DNA-binding protein from skeletal-muscle extracts that binds to probes of three muscle gene DNA elements is identified. This protein, referred to as muscle factor 3, forms the predominant nucleoprotein complex with the MCAT gene sequence motif in an electrophoretic mobility shift assay. This protein also binds to the skeletal actin muscle regulatory element, which contains the conserved CArG motif, and to a creatine kinase enhancer probe, which contains the E-box motif, a MyoD-binding site. Muscle factor 3 has a potent sequence-specific, single-stranded-DNA-binding activity. The specificity of this interaction was demonstrated by sequence-specific competition and by mutations that diminished or eliminated detectable complex formation. MyoD, a myogenic determination factor that is distinct from muscle factor 3, also bound to single-stranded-DNA probes in a sequence-specific manner, but other transcription factors did not. Multiple copies of the MCAT motif activated the expression of a heterologous promoter, and a mutation that eliminated expression was correlated with diminished factor binding. Muscle factor 3 and MyoD may be members of a class of DNA-binding proteins that modulate gene expression by their abilities to recognize DNA with unusual secondary structure in addition to specific sequence.

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Stimulation of Reca Protein Dependent Strand Assimilation and DNA Complex Formation by Single-Stranded DNA Binding Proteins

New Approaches in Eukaryotic DNA Replication ◽

10.1007/978-1-4684-4397-4_16 ◽

1983 ◽

pp. 333-341 ◽

Cited By ~ 1

Author(s):

George M. Weinstock ◽

Kevin McEntee ◽

I. Robert Lehman

Keyword(s):

Dna Binding ◽

Complex Formation ◽

Binding Proteins ◽

Reca Protein ◽

Dna Binding Proteins ◽

Single Stranded Dna ◽

Dna Complex ◽

Stimulation Of

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Identification of single-stranded-DNA-binding proteins that interact with muscle gene elements.

Molecular and Cellular Biology ◽

10.1128/mcb.11.4.1944 ◽

1991 ◽

Vol 11 (4) ◽

pp. 1944-1953 ◽

Cited By ~ 42

Author(s):

I M Santoro ◽

T M Yi ◽

K Walsh

Keyword(s):

Dna Binding ◽

Binding Proteins ◽

Regulatory Element ◽

Dna Binding Proteins ◽

Binding Activity ◽

Sequence Motif ◽

Mobility Shift ◽

Specific Sequence ◽

Single Stranded Dna ◽

Muscle Gene

A sequence-specific DNA-binding protein from skeletal-muscle extracts that binds to probes of three muscle gene DNA elements is identified. This protein, referred to as muscle factor 3, forms the predominant nucleoprotein complex with the MCAT gene sequence motif in an electrophoretic mobility shift assay. This protein also binds to the skeletal actin muscle regulatory element, which contains the conserved CArG motif, and to a creatine kinase enhancer probe, which contains the E-box motif, a MyoD-binding site. Muscle factor 3 has a potent sequence-specific, single-stranded-DNA-binding activity. The specificity of this interaction was demonstrated by sequence-specific competition and by mutations that diminished or eliminated detectable complex formation. MyoD, a myogenic determination factor that is distinct from muscle factor 3, also bound to single-stranded-DNA probes in a sequence-specific manner, but other transcription factors did not. Multiple copies of the MCAT motif activated the expression of a heterologous promoter, and a mutation that eliminated expression was correlated with diminished factor binding. Muscle factor 3 and MyoD may be members of a class of DNA-binding proteins that modulate gene expression by their abilities to recognize DNA with unusual secondary structure in addition to specific sequence.

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Cell rounding causes genomic instability by dissociation of single-stranded DNA-binding proteins

10.1101/463653 ◽

2018 ◽

Author(s):

Qian Guo ◽

Xianglu Liao ◽

Xingwu Wang ◽

Ling Liu ◽

Bao Song

Keyword(s):

Stem Cell ◽

Dna Binding ◽

Cell Therapy ◽

Genomic Instability ◽

Stem Cell Therapy ◽

Binding Proteins ◽

Dna Binding Proteins ◽

Single Stranded Dna ◽

Cell Rounding ◽

Wide Range

AbstractGenomic instability can cause a wide range of diseases, including cancer and cellular senescence, which is also a major challenge in stem cell therapy. However, how a single event can cause extremely high levels of genomic instability remains unclear. Using our developed method, cell in situ electrophoresis (CISE), and models of normal, cancer, and embryonic stem cells, we found that cell rounding as a catastrophic source event ubiquitously observed in vivo and in vitro might lead to large-scale DNA deprotection, genomic instability, chromosomal shattering, cell heterogeneity, and senescent crisis by dissociation of single-stranded DNA-binding proteins (SSBs). Understanding the mechanism may facilitate the development of clinical strategies for cancer therapy, improve the safety of stem cell therapy, and prevent pathological aging.

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