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Single-Strand DNA Binding Proteins01:03

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For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
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The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
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DNA unwinding helicase enzymes are a type of motor protein. Motor proteins can translocate along filaments or polymers using energy generated from ATP hydrolysis. Helicases are involved in all the important cellular processes where DNA unwinding is required, such as DNA replication, repair, recombination, and transcription. They are present in all living organisms, but vary in their structure, function, and mechanism of action. For example, in prokaryotes, DnaB helicase binds and translocates...
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Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
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Acetylation-dependent function of human single-stranded DNA binding protein 1.

Yuanzhong Wu1, Hongxia Chen2, Jinping Lu3

  • 1Sun Yat-sen University Cancer Center, State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Guangzhou 510060, China.

Nucleic Acids Research
|July 15, 2015
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Summary

Human single-stranded DNA binding protein 1 (hSSB1) acetylation at K94 by p300 prevents its degradation, enhancing DNA damage repair and cancer cell survival. Inhibiting acetylation boosts chemotherapy effectiveness.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cancer Research

Background:

  • Human single-stranded DNA binding protein 1 (hSSB1) is vital for DNA damage response and genome stability.
  • Regulatory mechanisms controlling hSSB1 function are not well understood.

Purpose of the Study:

  • To investigate the regulatory role of hSSB1 acetylation in DNA damage response.
  • To explore the therapeutic potential of targeting hSSB1 acetylation in cancer treatment.

Main Methods:

  • Site-directed mutagenesis to create hSSB1-K94R mutant.
  • Western blotting to detect protein levels and acetylation.
  • Cell viability assays post-treatment with DNA-damaging agents and inhibitors.
  • Analysis of clinical colorectal cancer samples.

Main Results:

  • Acetylation of hSSB1 at K94 by p300 inhibits its proteasomal degradation, mediated by SIRT4 and HDAC10.
  • The hSSB1-K94R mutant exhibits reduced cell survival following DNA damage.
  • Inhibition of p300/CBP with C646 increases cancer cell sensitivity to chemotherapy.
  • A positive correlation exists between hSSB1 and p300 levels in colorectal cancer patients.

Conclusions:

  • Acetylation is a novel regulatory mechanism critical for hSSB1 function in DNA repair and cell survival.
  • Targeting hSSB1 acetylation, potentially with p300/CBP inhibitors, represents a promising strategy to enhance chemotherapy efficacy in cancer patients.