Arm-site binding by lambda -integrase: solution structure and functional characterization of its amino-terminal domain

Proceedings of the National Academy of Sciences of the United States of America
J M WojciakRobert T Clubb

Abstract

The integrase protein (Int) from bacteriophage lambda catalyzes the insertion and excision of the viral genome into and out of Escherichia coli. It is a member of the lambda-Int family of site-specific recombinases that catalyze a diverse array of DNA rearrangements in archaebacteria, eubacteria, and yeast and belongs to the subset of this family that possesses two autonomous DNA-binding domains. The heterobivalent properties of Int can be decomposed into a carboxyl-terminal domain that executes the DNA cleavage and ligation reactions and a smaller amino-terminal domain that binds to an array of conserved DNA sites within the phage arms, thereby arranging Int protomers within the higher-order recombinogenic complex. We have determined that residues Met-1 to Leu-64 of Int constitute the minimal arm-type DNA-binding domain (INT-DBD(1-64)) and solved the solution structure by using NMR. We show that the INT-DBD(1-64) is a novel member of the growing family of three-stranded beta-sheet DNA-binding proteins, because it supplements this motif with a disordered amino-terminal basic tail that is important for arm-site binding. A model of the arm-DNA-binding domain recognizing its cognate DNA site is proposed on the basis of similaritie...Continue Reading

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Citations

May 7, 2010·Medical Microbiology and Immunology·Ulrich DobrindtJ Hacker
Apr 7, 2004·Journal of Molecular Biology·My D SamRobert T Clubb
Dec 4, 2002·Journal of Molecular Biology·Michael TekleSimone E Nunes-Düby
Dec 4, 2002·Journal of Molecular Biology·Dibyendu SarkarArthur Landy
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Sep 10, 2009·The Journal of Biological Chemistry·Aleksandra SzwagierczakAlexander Rakin
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Mar 9, 2005·Proceedings of the National Academy of Sciences of the United States of America·Marta Radman-LivajaArthur Landy
Aug 13, 2014·Proceedings of the National Academy of Sciences of the United States of America·Wenjun TongArthur Landy
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