Physical and Functional Interactions between 3-Methyladenine DNA Glycosylase and Topoisomerase I in Mycobacteria

被引：2
|
作者：
Yang, Qiong [1 ]
Huang, Feng [1 ]
Hu, Lihua [1 ]
He, Zheng-Guo [1 ]
机构：
[1] Huazhong Agr Univ, Coll Life Sci & Technol, Ctr Prote Res, Natl Key Lab Agr Microbiol, Wuhan 430070, Peoples R China
来源：
BIOCHEMISTRY-MOSCOW | 2012年 / 77卷 / 04期
基金：
中国国家自然科学基金;
关键词：
Mycobacterium tuberculosis; DNA glycosylase; topoisomerase I; DNA repair; SACCHAROMYCES-CEREVISIAE; ESCHERICHIA-COLI; SUBSTRATE-SPECIFICITY; BINDING PROTEIN; BASE EXCISION; TUBERCULOSIS; REPAIR; POLYMERASE; SEQUENCE; DAMAGE;
D O I：
10.1134/S0006297912040098
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
DNA glycosylases play important roles in DNA repair in a variety of organisms, including humans. However, the function and regulation of these enzymes in the pathogenic bacterium Mycobacterium tuberculosis and related species are poorly understood. In the present study, the physical and functional interactions between 3-methyladenine DNA glycosylase (MAG) and topoisomerase I (TopA) in M. tuberculosis and M. smegmatis were characterized. MAG was found to inhibit the function of TopA in relaxing supercoiled DNA. In contrast, TopA stimulated the cleavage function of MAG on a damaged DNA substrate that contains hypoxanthine. The interaction between the two proteins was conserved between the two mycobacterial species. Several mutations in MAG that led to the loss of its interaction with and activity regulation of TopA were also characterized. The results of this study further elucidate glycosylase regulation in both M. smegmatis and M. tuberculosis.
引用
收藏
页码：378 / 387
页数：10
相关论文
共 50 条
  • [1] Physical and functional interactions between 3-methyladenine DNA glycosylase and topoisomerase I in mycobacteria
    Qiong Yang
    Feng Huang
    Lihua Hu
    Zheng-Guo He
    Biochemistry (Moscow), 2012, 77 : 378 - 387
  • [2] THE RELEASE OF 3-METHYLADENINE FROM NUCLEOSOMAL DNA BY A 3-METHYLADENINE DNA GLYCOSYLASE
    PRICE, JA
    HELLER, E
    GOLDTHWAIT, DA
    CARCINOGENESIS, 1983, 4 (02) : 145 - 152
  • [3] MODEL FOR A RECOGNITION OF 3-METHYLADENINE BY 3-METHYLADENINE DNA GLYCOSYLASE - THE STACKING INTERACTION BETWEEN 3-METHYLADENINE AND INDOLE RINGS
    YAMAGATA, Y
    KATO, M
    FUJII, S
    CHEMICAL & PHARMACEUTICAL BULLETIN, 1994, 42 (11) : 2385 - 2387
  • [4] A model for 3-methyladenine recognition by 3-methyladenine DNA glycosylase I (TAG) from Staphylococcus aureus
    Zhu, Xiaofeng
    Yan, Xuan
    Carter, Lester G.
    Liu, Huanting
    Graham, Shirley
    Coote, Peter J.
    Naismith, James
    ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 2012, 68 : 610 - 615
  • [5] DNA damage recognition and repair by 3-methyladenine DNA glycosylase I (TAG)
    Metz, Audrey H.
    Hollis, Thomas
    Eichman, Brandt F.
    EMBO JOURNAL, 2007, 26 (09): : 2411 - 2420
  • [6] REPAIR OF NUCLEOSOMAL DNA INVITRO BY A 3-METHYLADENINE DNA GLYCOSYLASE
    PRICE, JA
    HELLER, E
    GOLDTHWAIT, DA
    FEDERATION PROCEEDINGS, 1981, 40 (06) : 1768 - 1768
  • [7] REPAIR OF NUCLEOSOMAL DNA INVITRO BY A 3-METHYLADENINE DNA GLYCOSYLASE
    PRICE, JA
    HELLER, E
    GOLDTHWAIT, DA
    PROCEEDINGS OF THE AMERICAN ASSOCIATION FOR CANCER RESEARCH, 1981, 22 (MAR): : 88 - 88
  • [8] 1,N-6-ETHENOADENINE IS PREFERRED OVER 3-METHYLADENINE AS SUBSTRATE BY A CLONED HUMAN N-METHYLPURINE DNA GLYCOSYLASE (3-METHYLADENINE DNA GLYCOSYLASE)
    DOSANJH, MK
    ROY, R
    MITRA, S
    SINGER, B
    BIOCHEMISTRY, 1994, 33 (07) : 1624 - 1628
  • [9] A novel zinc snap motif conveys structural stability to 3-methyladenine DNA glycosylase I
    Kwon, K
    Cao, CY
    Stivers, JT
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (21) : 19442 - 19446
  • [10] PROTECTION AGAINST CHLOROETHYLNITROSOUREA CYTOTOXICITY BY EUKARYOTIC 3-METHYLADENINE DNA GLYCOSYLASE
    MATIJASEVIC, Z
    BOOSALIS, M
    MACKAY, W
    SAMSON, L
    LUDLUM, DB
    PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (24) : 11855 - 11859
12345