期刊
PROTEIN SCIENCE
卷 13, 期 11, 页码 3043-3050出版社
WILEY
DOI: 10.1110/ps.04911804
关键词
biotin rotein ligase; protein modification; biotinylation; acyl adenylate; BirA
资金
- NIAID NIH HHS [AI 15650, R37 AI015650, R01 AI015650] Funding Source: Medline
Biotin protein ligases (BPLs) are enzymes of extraordinary specificity. BirA, the BPL of Escherichia coli biotinylates only a single cellular protein. We report a mutant BirA that attaches biotin to a large number of cellular proteins in vivo and to bovine serum albumin, chloramphenicol acetyltransferase, immunoglobin heavy and light chains, and RNAse A in vitro. The mutant BirA also self biotinylates in vivo and in vitro. The wild type BirA protein is much less active in these reactions. The biotinylation reaction is proximitydependent in that a greater extent of biotinylation was seen when the mutant ligase was coupled to the acceptor proteins than when the acceptors were free in solution. This approach may permit facile detection and recovery of interacting proteins by existing avidin/streptavidin technology.
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