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J Virol, February 1998, p. 900-909, Vol. 72, No. 2
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Characterization of the DNA-Binding Domain of the Avian Y-Box Protein, chkYB-2, and Mutational Analysis of Its Single-Strand Binding Motif in the Rous Sarcoma Virus Enhancer

Ashok Nambiar, S. K. Swamynathan, Jagannadha C. Kandala, and Ramareddy V. Guntaka*

Molecular Microbiology and Immunology, University of Missouri--- Columbia School of Medicine, Columbia, Missouri 65212

Received 2 September 1997/Accepted 15 October 1997

chkYB-2 is a sequence-specific, single-stranded DNA binding chicken Y-box protein that promotes Rous sarcoma virus long terminal repeat (RSV LTR)-driven transcription in avian fibroblasts. The DNA-binding domain of chkYB-2 has been mapped by characterizing the DNA binding properties of purified recombinant chkYB-2 mutant polypeptides. The data indicate that the invariant cold shock domain (CSD) is necessary but not sufficient for association with DNA and suggest that another conserved region, adjacent to the carboxyl boundary of the CSD, plays a role in high-affinity DNA binding. chkYB-2 binds to a tandem repeat of the 5'-GTACCACC-3' motif on the RSV LTR. Mutational analysis of this recognition sequence revealed the requirement of an essentially unaltered template for both high-affinity binding by chkYB-2 as well as maximal transcriptional activity of the RSV LTR in vivo. The single-stranded DNA binding activity of chkYB-2 is augmented by Mg2+. The possible significance of this finding for transactivation by a single-strand DNA binding protein is discussed.

* Corresponding author. Mailing address: Molecular Microbiology and Immunology, University of Missouri---Columbia School of Medicine, M616 Medical Sciences Bldg., Columbia, MO 65212. Phone: (573) 882-7139. Fax: (573) 882-4287. E-mail: guntaka{at}showme.missouri.edu.




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