Regulation of double-strand break-induced mammalian homologous recombination by UBL1, a RAD51-interacting protein

Wenhui Li, Bahar Hesabi, Angela Babbo, Carol Pacione, Jingmei Liu, David J. Chen, Jac A. Nickoloff, Zhiyuan Shen

Research output: Contribution to journalArticle

63 Citations (Scopus)

Abstract

Mammalian RAD51 protein plays essential roles in DNA homologous recombination, DNA repair and cell proliferation. RAD51 activities are regulated by its associated proteins. It was previously reported that a ubiquitin-like protein, UBL1, associates with RAD51 in the yeast two-hybrid system. One function of UBL1 is to covalently conjugate with target proteins and thus modify their function. In the present study we found that non-conjugated UBL1 forms a complex with RAD51 and RAD52 proteins in human cells. Overexpression of UBL1 down-regulates DNA double-strand break-induced homologous recombination in CHO cells and reduces cellular resistance to ionizing radiation in HT1080 cells. With or without overexpressed UBL1, most homologous recombination products arise by gene conversion. However, overexpression of UBL1 reduces the fraction of bidirectional gene conversion tracts. Overexpression of a mutant UBL1 that is incapable of being conjugated retains the ability to inhibit homologous recombination. These results suggest a regulatory role for UBL1 in homologous recombination.

Original languageEnglish (US)
Pages (from-to)1145-1153
Number of pages9
JournalNucleic Acids Research
Volume28
Issue number5
StatePublished - Mar 1 2000

Fingerprint

Rad51 Recombinase
Homologous Recombination
Gene Conversion
Ubiquitins
Recombinational DNA Repair
Two-Hybrid System Techniques
Double-Stranded DNA Breaks
CHO Cells
Ionizing Radiation
Proteins
Down-Regulation
Cell Proliferation
DNA

ASJC Scopus subject areas

  • Genetics

Cite this

Li, W., Hesabi, B., Babbo, A., Pacione, C., Liu, J., Chen, D. J., ... Shen, Z. (2000). Regulation of double-strand break-induced mammalian homologous recombination by UBL1, a RAD51-interacting protein. Nucleic Acids Research, 28(5), 1145-1153.

Regulation of double-strand break-induced mammalian homologous recombination by UBL1, a RAD51-interacting protein. / Li, Wenhui; Hesabi, Bahar; Babbo, Angela; Pacione, Carol; Liu, Jingmei; Chen, David J.; Nickoloff, Jac A.; Shen, Zhiyuan.

In: Nucleic Acids Research, Vol. 28, No. 5, 01.03.2000, p. 1145-1153.

Research output: Contribution to journalArticle

Li, W, Hesabi, B, Babbo, A, Pacione, C, Liu, J, Chen, DJ, Nickoloff, JA & Shen, Z 2000, 'Regulation of double-strand break-induced mammalian homologous recombination by UBL1, a RAD51-interacting protein', Nucleic Acids Research, vol. 28, no. 5, pp. 1145-1153.
Li, Wenhui ; Hesabi, Bahar ; Babbo, Angela ; Pacione, Carol ; Liu, Jingmei ; Chen, David J. ; Nickoloff, Jac A. ; Shen, Zhiyuan. / Regulation of double-strand break-induced mammalian homologous recombination by UBL1, a RAD51-interacting protein. In: Nucleic Acids Research. 2000 ; Vol. 28, No. 5. pp. 1145-1153.
@article{6a5c126a70774fc2a9e2935d4c457298,
title = "Regulation of double-strand break-induced mammalian homologous recombination by UBL1, a RAD51-interacting protein",
abstract = "Mammalian RAD51 protein plays essential roles in DNA homologous recombination, DNA repair and cell proliferation. RAD51 activities are regulated by its associated proteins. It was previously reported that a ubiquitin-like protein, UBL1, associates with RAD51 in the yeast two-hybrid system. One function of UBL1 is to covalently conjugate with target proteins and thus modify their function. In the present study we found that non-conjugated UBL1 forms a complex with RAD51 and RAD52 proteins in human cells. Overexpression of UBL1 down-regulates DNA double-strand break-induced homologous recombination in CHO cells and reduces cellular resistance to ionizing radiation in HT1080 cells. With or without overexpressed UBL1, most homologous recombination products arise by gene conversion. However, overexpression of UBL1 reduces the fraction of bidirectional gene conversion tracts. Overexpression of a mutant UBL1 that is incapable of being conjugated retains the ability to inhibit homologous recombination. These results suggest a regulatory role for UBL1 in homologous recombination.",
author = "Wenhui Li and Bahar Hesabi and Angela Babbo and Carol Pacione and Jingmei Liu and Chen, {David J.} and Nickoloff, {Jac A.} and Zhiyuan Shen",
year = "2000",
month = "3",
day = "1",
language = "English (US)",
volume = "28",
pages = "1145--1153",
journal = "Nucleic Acids Research",
issn = "0305-1048",
publisher = "Oxford University Press",
number = "5",

}

TY - JOUR

T1 - Regulation of double-strand break-induced mammalian homologous recombination by UBL1, a RAD51-interacting protein

AU - Li, Wenhui

AU - Hesabi, Bahar

AU - Babbo, Angela

AU - Pacione, Carol

AU - Liu, Jingmei

AU - Chen, David J.

AU - Nickoloff, Jac A.

AU - Shen, Zhiyuan

PY - 2000/3/1

Y1 - 2000/3/1

N2 - Mammalian RAD51 protein plays essential roles in DNA homologous recombination, DNA repair and cell proliferation. RAD51 activities are regulated by its associated proteins. It was previously reported that a ubiquitin-like protein, UBL1, associates with RAD51 in the yeast two-hybrid system. One function of UBL1 is to covalently conjugate with target proteins and thus modify their function. In the present study we found that non-conjugated UBL1 forms a complex with RAD51 and RAD52 proteins in human cells. Overexpression of UBL1 down-regulates DNA double-strand break-induced homologous recombination in CHO cells and reduces cellular resistance to ionizing radiation in HT1080 cells. With or without overexpressed UBL1, most homologous recombination products arise by gene conversion. However, overexpression of UBL1 reduces the fraction of bidirectional gene conversion tracts. Overexpression of a mutant UBL1 that is incapable of being conjugated retains the ability to inhibit homologous recombination. These results suggest a regulatory role for UBL1 in homologous recombination.

AB - Mammalian RAD51 protein plays essential roles in DNA homologous recombination, DNA repair and cell proliferation. RAD51 activities are regulated by its associated proteins. It was previously reported that a ubiquitin-like protein, UBL1, associates with RAD51 in the yeast two-hybrid system. One function of UBL1 is to covalently conjugate with target proteins and thus modify their function. In the present study we found that non-conjugated UBL1 forms a complex with RAD51 and RAD52 proteins in human cells. Overexpression of UBL1 down-regulates DNA double-strand break-induced homologous recombination in CHO cells and reduces cellular resistance to ionizing radiation in HT1080 cells. With or without overexpressed UBL1, most homologous recombination products arise by gene conversion. However, overexpression of UBL1 reduces the fraction of bidirectional gene conversion tracts. Overexpression of a mutant UBL1 that is incapable of being conjugated retains the ability to inhibit homologous recombination. These results suggest a regulatory role for UBL1 in homologous recombination.

UR - http://www.scopus.com/inward/record.url?scp=0034159893&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034159893&partnerID=8YFLogxK

M3 - Article

C2 - 10666456

AN - SCOPUS:0034159893

VL - 28

SP - 1145

EP - 1153

JO - Nucleic Acids Research

JF - Nucleic Acids Research

SN - 0305-1048

IS - 5

ER -