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Accession number;04A0258598
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| Title;Molecular structure of Sensory part of VnfA, Nitrogenase transcriptional regulator in Azotobacter vinelandii. |
| Author;
NAKAJIMA HIROSHI
(Meidai In)
AONO SHIGETOSHI
(Okazakikiko Togobaio)
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Journal Title;Abstracts. Symposium on Biofunctional Chemistry
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Journal Code:L0836A
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ISSN:
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VOL.18th;NO.;PAGE.30-31(2003)
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| Figure&Table&Reference;FIG.1 |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;VnfA is one of transcriptional regulators involved in diazotroph Azotobacter vinelandii. Although VnfA is known to bind to an upstream sequence of vnf operon to activate the expression of nitrogenase-2, vanadium nitrogenase, molecular mechanism of the regulation, for instance effecter molecules and molecular structure of the sensory part, remains unclear. In the present study, we will show that VnfA includes an iron-sulfur cluster as a prosthetic group both in vivo and in vitro. Transcriptionally active VnfA contains the [3Fe-4S]+ type cluster which is similar to that observed in cytoplasmic aconitase. Decomposition of the cluster results in decrease in the transcriptional activity by 80%, indicating formation and decomposition of the cluster is one of the control mechanism of VnfA activity. The other control mechanism might be a reaction of the 3Fe-4S cluster with Fe ion because addition of Fe ion causes the partial depression of VnfA activity. Detail analysis for this control mechanism is now in progress. (author abst.) |
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