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Originally published In Press as doi:10.1074/jbc.M100393200 on February 27, 2001

J. Biol. Chem., Vol. 276, Issue 20, 16992-16997, May 18, 2001
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Chimeras between Single-stranded DNA-binding Proteins from Escherichia coli and Mycobacterium tuberculosis Reveal That Their C-terminal Domains Interact with Uracil DNA Glycosylases*

Priya HandaDagger , Narottam Acharya, and Umesh Varshney§

From the Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore, 560 012, India

Uracil, a promutagenic base in DNA can arise by spontaneous deamination of cytosine or incorporation of dUMP by DNA polymerase. Uracil is removed from DNA by uracil DNA glycosylase (UDG), the first enzyme in the uracil excision repair pathway. We recently reported that the Escherichia coli single-stranded DNA binding protein (SSB) facilitated uracil excision from certain structured substrates by E. coli UDG (EcoUDG) and suggested the existence of interaction between SSB and UDG. In this study, we have made use of the chimeric proteins obtained by fusion of N- and C-terminal domains of SSBs from E. coli and Mycobacterium tuberculosis to investigate interactions between SSBs and UDGs. The EcoSSB or a chimera containing its C-terminal domain interacts with EcoUDG in a binary (SSB-UDG) or a ternary (DNA-SSB-UDG) complex. However, the chimera containing the N-terminal domain from EcoSSB showed no interactions with EcoUDG. Thus, the C-terminal domain (48 amino acids) of EcoSSB is necessary and sufficient for interaction with EcoUDG. The data also suggest that the C-terminal domain (34 amino acids) of MtuSSB is a predominant determinant for mediating its interaction with MtuUDG. The mechanism of how the interactions between SSB and UDG could be important in uracil excision repair pathway has been discussed.

* This work was supported in part by research grants from the Council of Scientific and Industrial Research, the Department of Biotechnology, and the Department of Science and Technology, New Delhi, India.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Supported by a senior research fellowship from the Council of Scientific and Industrial Research.

§ To whom correspondence should be addressed. Tel.: 91-80-309-2686; Fax: 91-80-360-2697 or 91-80-360-0683; E-mail: varshney@mcbl.iisc.ernet.in.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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