A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
AtCYP20-2 is an auxiliary protein of the chloroplast NAD(P)H dehydrogenase complex
Tekijät: Sirpio S, Holmstrom M, Battchikova N, Aro EM
Kustantaja: ELSEVIER SCIENCE BV
Julkaisuvuosi: 2009
Lehti:: FEBS Letters
Tietokannassa oleva lehden nimi: FEBS LETTERS
Lehden akronyymi: FEBS LETT
Vuosikerta: 583
Numero: 14
Aloitussivu: 2355
Lopetussivu: 2358
Sivujen määrä: 4
ISSN: 0014-5793
DOI: https://doi.org/10.1016/j.febslet.2009.06.031
Tiivistelmä
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.
Turun yliopiston Tutkimustietojärjestelmän portaali