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PMID:23085540
| Citation |
Rotem, O, Biran, D and Ron, EZ (2013) Methionine biosynthesis in Agrobacterium tumefaciens: study of the first enzyme. Res. Microbiol. 164:12-6 |
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| Abstract |
Here we characterize the first step in methionine biosynthesis in Agrobacterium tumefaciens, an α-proteobacterium. We explored the metA gene and its products and found several unique properties. Although the gene was annotated as a homoserine transsuccinylase, based upon sequence similarity to characterized homologs in other bacteria, including Escherichia coli, the enzyme uses acetyl-CoA as a substrate and therefore is functionally a transacetylase. Moreover, the protein is thermolabile and the gene is under regulation of heat shock transcriptional activator σ32. 3. The gene has a SAM-riboswitch, which shuts off transcription by σ-32 as well as by the vegetative σ-70. |
| Links |
PubMed Online version:10.1016/j.resmic.2012.10.005 |
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Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
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Contributes to |
GO:0006508: proteolysis |
ECO:0000269: |
P |
The protein is a proteolysis substrate and has high degradation at high temperatures. In Figure 5 it was determined whether or not the metA gene of A. tumefaciens is induced at elevated temperatures. It was found that that there was no induction in the absence of the heat shock transcriptional activator. |
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See also
References
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