en
Scientific article
Open access
English

Phage Mu transposase: deletion of the carboxy-terminal end does not abolish DNA-binding activity

Published inMolecular and General Genetics, vol. 210, no. 1, p. 77-85
Publication date1987
Abstract

We demonstrate that a specific site on the transposase protein, pA, of bacteriophage Mu is highly susceptible to proteolytic cleavage. Cleavage is observed in a minicell system on solubilisation with the non-ionic detergent Triton X-100 or following addition of a solubilised minicell preparation to pA synthesised in a cell-free coupled transcription/translation system. Cleavage occurs at the carboxy-terminal end of the protein and generates a truncated polypeptide of 64 kDa, pA*, which retains some of the DNA-binding properties of pA. These results suggest that pA may be divided into functional domains for DNA binding and for interaction with the proteins involved in phage replication.

Keywords
  • Phage Mu transposase
  • Processing
  • Protein domains
  • DNA binding
Citation (ISO format)
BETERMIER, M. et al. Phage Mu transposase: deletion of the carboxy-terminal end does not abolish DNA-binding activity. In: Molecular and General Genetics, 1987, vol. 210, n° 1, p. 77–85. doi: 10.1007/BF00337761
Main files (1)
Article (Published version)
Identifiers
ISSN of the journal0026-8925
125views
103downloads

Technical informations

Creation02/16/2021 11:06:00 AM
First validation02/16/2021 11:06:00 AM
Update time03/16/2023 12:06:23 AM
Status update03/16/2023 12:06:23 AM
Last indexation02/12/2024 12:02:10 PM
All rights reserved by Archive ouverte UNIGE and the University of GenevaunigeBlack