Ontology type: schema:ScholarlyArticle
1987-11
AUTHORSM. Betermier, R. Alazard, F. Ragueh, E. Roulet, A. Toussaint, M. Chandler
ABSTRACTWe 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. More... »
PAGES77-85
http://scigraph.springernature.com/pub.10.1007/bf00337761
DOIhttp://dx.doi.org/10.1007/bf00337761
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PUBMEDhttps://www.ncbi.nlm.nih.gov/pubmed/2828889
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