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FOR THE RECORD

HU- binds to the putative double-stranded DNA mimic HI1450 from Haemophilus influenzae

Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, Rockville, Maryland 20850, USA

(RECEIVED December 7, 2004; FINAL REVISION March 14, 2005; ACCEPTED March 21, 2005)

Recently, the solution structure of the hypothetical protein HI1450 from Haemophilus influenzae was solved as part of a structure-based effort to understand function. The distribution of its many negatively charged residues and weak structure and sequence homology to uracil DNA glycosylase inhibitor (Ugi) suggested that HI1450 may act as a double-stranded DNA (dsDNA) mimic. We present supporting evidence here and show that HI1450 interacts with the dsDNA-binding protein HU-. The interaction between HI1450 and HU- from H. influenzae is characterized using calorimetry and NMR spectroscopy. HU- binds to HI1450 with a K_d of 3.0 ± 0.2 µM, which is similar in affinity to its interaction with dsDNA. Chemical shift perturbation data indicate that the 1-strand of HI1450 and neighboring regions are most directly involved in interactions with HU-. These results show that HI1450 and its structural homolog, Ugi, use similar parts of their structures to recognize DNA-binding proteins.

Keywords: double-stranded DNA mimic; HU-; structural genomics

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.041275705.

Reprint requests to: John Orban, Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, 9600 Gudelsky Drive, Rockville, MD 20850, USA; e-mail: orban{at}umbi.umd.edu; fax: (301) 738-6255.

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