1887

Abstract

The glycine cleavage enzyme system, encoded by the operon, catalyses the oxidative cleavage of glycine to CO, NH and a one-carbon methylene group. Transcription of the operon is positively regulated by GcvA and negatively regulated by GcvA and GcvR. Using a LexA-based system for analysing protein heterodimerization, it is shown that GcvR interacts directly with GcvA to repress expression. Several mutations in either or that result in a loss of repression also result in a loss of GcvA/GcvR heterodimerization. Finally, it is shown that the C-terminal half of GcvA is involved in its interaction with GcvR, whilst the entire GcvR protein appears to be necessary for heterodimerization.

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2001-08-01
2024-04-26
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