Rubredoxin A

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Rubredoxin A (RubA) is a protein conserved across all studied oxygenic photoautotrophs. [1]

Contents

Structure

As of March 2015 there was no crystal structure of RubA although a structure of the homologous protein from a cryptomonad was determined using NMR. [2] Investigation of the gene however indicates that it differs from other known rubredoxins in being bound to the thylakoid membrane via a C-terminal transmembrane helix. [1] [3] [4]

Function

An investigation of Guillardia theta noted that RubA had a similar distribution to Photosystem II (PSII) and immunological experiments indicated the presence of RubA in PSII complexes isolated from Spinacia oleracea . [3] In Synechocystis sp. PCC 6803 it has been demonstrated that the insertion of an antibiotic cassette into the rubA gene results in a marked decrease in the amount of PSII present, [1] while the same mutation within Chlamydomonas reinhardtii and in Arabidopsis thaliana results in a total absence of PSII. [1]

Conversely, another study performed in Synechococcus sp. PCC 7002 indicated that mutation of the rubA gene interfered with iron-sulphur cluster assembly in Photosystem I (PSI), rather than affecting PSII. [4] [5]

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Avadhesha Surolia is a glycobiologist at the Indian Institute of Science (IISc), Bangalore. He was born in Kishangarh, Rajasthan, India. Presently, he is an honorary professor at the Molecular Biophysics Unit, IISc and holds the Bhatnagar fellowship of the Council of Scientific and Industrial Research (CSIR). He is known for his work on lectin structure and interactions, orientation and dynamics of cell surface carbohydrate receptors and protein folding, diabetes, antimalarials and anti-cancer agents based on curcumin, flavonoids, etc. In addition, neuropathic pain, neurodegenerative disorders and the link between immunity and obsessive–compulsive disorder are areas of his current interest

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References

  1. 1 2 3 4 Calderon, R. H., García-Cerdán, J. G., Malnoë, A., Cook, R., Russell, J. J., Gaw, C., Dent, R. M., de Vitry, C. and Niyogi, K. K. (July 2013). "A Conserved Rubredoxin Is Necessary for Photosystem II Accumulation in Diverse Oxygenic Photoautotrophs". The Journal of Biological Chemistry. 288 (37): 26688–26696. doi: 10.1074/jbc.M113.487629 . PMC   3772215 . PMID   23900844.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  2. Schweimer, K., Hoffmann, S., Wastl, J., Maier, U.G., Rösch, P., and Sticht H. (2000). "Solution structure of a zinc substituted eukaryotic rubredoxin from the cryptomonad alga "Guillardia theta"". Protein Science. 9 (8): 1474–1486. doi:10.1110/ps.9.8.1474. PMC   2144721 . PMID   10975569.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  3. 1 2 Wastl, J., Duin, E. C., Iuzzolino, L., Dörner, W., Link. T., Dau, H., Lingelbach, K. and Maier U. G. (2000). "Eukaryotically Encoded and Chloroplast-located Rubredoxin Is Associated with Photosystem II". The Journal of Biological Chemistry. 275 (39): 30058–30068. doi: 10.1074/jbc.M004629200 . PMID   10878021.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  4. 1 2 Shen, G., Zhao, J., Reimer, S. K., Antonkine, M. L., Cai, Q., Weiland, S. M., Golbeck, J. H. and Bryant, D. A. (2002). "Assembly of Photosystem II: I. Inactivation of The rubA Gene Encoding A Membrane-Associated Rubredoxin In The Cyanobacterium Synechococcus sp. PCC 7002 Causes A Loss of Photosystem I Activity". The Journal of Biological Chemistry. 277 (23): 20343–20354. doi: 10.1074/jbc.M201103200 . PMID   11914373.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  5. Shen, G., Antonkine, M. L., van der Est, A., Vassiliev, I. R., Brettel, K., Bittl, R., Zech, S. G., Zhao, J., Stehlik, D., Bryant, D. A. and Golbeck, J. H. (2002). "Assembly of Photosystem I: II. Rubredoxin Is Required for the Assembly of Fx in Synechococcus sp. PCC 7002 As Shown by Optical and EPR Spectroscopy". The Journal of Biological Chemistry. 277 (23): 20355–20366. doi: 10.1074/jbc.M201104200 . PMID   11914374.{{cite journal}}: CS1 maint: multiple names: authors list (link)