Faculty Collaboration Database

Short peptide fragments derived from HMG-I/Y proteins bind specifically to the minor groove of DNA. Biochemistry 1994 May 03;33(17):5347-55

Date

05/03/1994

Pubmed ID

8172908

DOI

10.1021/bi00183a043

Scopus ID

2-s2.0-0028303273 (requires institutional sign-in at Scopus site)   97 Citations

Abstract

Short peptides derived from chromosomal proteins have previously been proposed to bind specifically to the minor groove of A,T-rich DNA [for a review, see M. E. A. Churchill and A. A. Travers (1991) Trends Biochem. Sci. 16, 92-97]. Using NMR spectroscopy, we investigated the DNA binding of SPRKSPRK, which is one such A,T-specific motif. Under the conditions studied SPRKSPRK interacts only nonspecifically with d(CGCAAAAAAGGC).d(GCCTTTTTTGCG). The peptides TPKRPRGRPKK, PRGRPKK, and PRGRP derived from the non-histone chromosomal protein HMG-I/Y, however, bind specifically to the central A,T sites of d(CGCAAATTTGCG)2 and d(CGCGAATTCGCG)2. 2D NOE measurements show that the RGR segment of each peptide is in contact with the minor groove. The arginine side chains and the peptide backbone are buried deep in the minor groove, in a fashion generally similar to the antibiotic netropsin. Under the same conditions the peptide PKGKP does not interact with the same oligonucleotide duplexes, indicating that the arginine guanidinium groups are major determinants of the A,T specificity.

Author List

Geierstanger BH, Volkman BF, Kremer W, Wemmer DE

Author

Brian F. Volkman PhD Professor in the Biochemistry department at Medical College of Wisconsin

MESH terms used to index this publication - Major topics in bold

Amino Acid Sequence
Base Sequence
Binding Sites
Carrier Proteins
Chromosomal Proteins, Non-Histone
DNA
Distamycins
High Mobility Group Proteins
Hydrogen Bonding
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular Sequence Data
Netropsin
Oligodeoxyribonucleotides
Oligopeptides
Peptide Fragments
X-Ray Diffraction