A1 Refereed original research article in a scientific journal
AtCYP20-2 is an auxiliary protein of the chloroplast NAD(P)H dehydrogenase complex
Authors: Sirpio S, Holmstrom M, Battchikova N, Aro EM
Publisher: ELSEVIER SCIENCE BV
Publication year: 2009
Journal:: FEBS Letters
Journal name in source: FEBS LETTERS
Journal acronym: FEBS LETT
Volume: 583
Issue: 14
First page : 2355
Last page: 2358
Number of pages: 4
ISSN: 0014-5793
DOI: https://doi.org/10.1016/j.febslet.2009.06.031
Abstract
AtCYP20-2 is one of 16 immunophilins in thylakoid lumen. The presence of the isomerase domain in AtCYP20-2, an enrichment of AtCYP20-2 in the stroma membranes and it's co-migration with NAD(P)H dehydrogenase (NDH) in native gels provide evidence that AtCYP20-2 is an auxiliary protein of NDH. When different NDH mutants were studied, AtCYP20-2 was found to be strongly reduced especially in mutants deficient in the membrane domain of NDH, thus suggesting a role in the assembly of NDH hydrophobic domain. Lack of AtCYP20-2, however, did not lead to severe malfunction of NDH, indicating redundancy in the function of lumenal immunophilins. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
AtCYP20-2 is one of 16 immunophilins in thylakoid lumen. The presence of the isomerase domain in AtCYP20-2, an enrichment of AtCYP20-2 in the stroma membranes and it's co-migration with NAD(P)H dehydrogenase (NDH) in native gels provide evidence that AtCYP20-2 is an auxiliary protein of NDH. When different NDH mutants were studied, AtCYP20-2 was found to be strongly reduced especially in mutants deficient in the membrane domain of NDH, thus suggesting a role in the assembly of NDH hydrophobic domain. Lack of AtCYP20-2, however, did not lead to severe malfunction of NDH, indicating redundancy in the function of lumenal immunophilins. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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