Two mutations of phage Mu transposase that affect strand transfer or interactions with B protein lie in distinct polypeptide domains
- 20 May 1991
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 219 (2) , 189-199
- https://doi.org/10.1016/0022-2836(91)90561-j
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- Efficient Mu transposition requires interaction of transposase with a DNA sequence at the Mu operator: Implications for regulationCell, 1989
- Interaction of distinct domains in Mu transposase with Mu DNA ends and an internal transpositional enhancerNature, 1989
- Target immunity of Mu transposition reflects a differential distribution of Mu B proteinCell, 1988
- Transposition of Mu DNA: Joining of Mu to target DNA can be uncoupled from cleavage at the ends of MuCell, 1987
- Transpososomes: Stable protein-DNA complexes involved in the in vitro transposition of bacteriophage Mu DNACell, 1987
- Carboxyl-terminal mutants of phage Mu transposaseJournal of Genetics, 1986
- Mechanism of transposition of bacteriophage Mu: structure of a transposition intermediateCell, 1985
- A truncated form of the bacteriophage Mu B protein promotes conservative integration, but not replicative Transposition, of Mu DNACell, 1985
- Interaction of recA protein with single-stranded DNAJournal of Molecular Biology, 1985
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970