Link to the University of Pittsburgh Homepage
Link to the University Library System Homepage Link to the Contact Us Form

Cooperativity mutants of the γδ resolvase identify an essential interdimer interaction

Hughes, RE and Hatfull, GF and Rice, P and Steitz, TA and Grindley, NDF (1990) Cooperativity mutants of the γδ resolvase identify an essential interdimer interaction. Cell, 63 (6). 1331 - 1338. ISSN 0092-8674

[img] Plain Text (licence)
Available under License : See the attached license file.

Download (1kB)


γδ resolvase, a transposon-encoded site-specific recombinase, catalyzes the resolution of the cointegrate intermediate of γδ transposition. The recombination reaction involves the formation of a catalytic nucleoprotein complex whose structure is determined by specific protein-DNA and protein-protein interactions. We have isolated many resolvase mutants and have identified four that are unable to mediate a subclass of higher order protein-protein interactions necessary for recombination. This mutant phenotype is characterized by an inability to catalyze recombination, a loss of cooperative binding to res DNA, and a failure to induce looping out of the DNA between two resolvase binding sites within res. The amino acid side chains identified by the cooperativity mutants cluster on a surface of the protein that mediates an interaction between resolvase dimers in a crystallographic tetramer. We have therefore identified a region of resolvase that mediates an interdimer protein-protein interaction necessary for the formation of the recombinogenic synaptic intermediate. © 1990.


Social Networking:
Share |


Item Type: Article
Status: Published
CreatorsEmailPitt UsernameORCID
Hughes, RE
Hatfull, GFgfh@pitt.eduGFH
Rice, P
Steitz, TA
Grindley, NDF
Date: 21 December 1990
Date Type: Publication
Journal or Publication Title: Cell
Volume: 63
Number: 6
Page Range: 1331 - 1338
DOI or Unique Handle: 10.1016/0092-8674(90)90428-h
Schools and Programs: Dietrich School of Arts and Sciences > Biological Sciences
Refereed: Yes
ISSN: 0092-8674
MeSH Headings: Amino Acid Sequence; Binding Sites; DNA Transposable Elements; Macromolecular Substances; Models, Molecular; Molecular Sequence Data; Mutagenesis; Nucleotidyltransferases--genetics; Nucleotidyltransferases--metabolism; Plasmids; Protein Conformation; Recombination, Genetic; Transposases
PubMed ID: 2175679
Date Deposited: 01 Mar 2013 15:28
Last Modified: 02 Feb 2019 15:57


Monthly Views for the past 3 years

Plum Analytics

Actions (login required)

View Item View Item