AI Article Synopsis
- AtCYP20-2 is an immunophilin located in the thylakoid lumen, shown to assist the NAD(P)H dehydrogenase (NDH) due to its presence and co-migration with NDH in experiments.
- Studies indicate that AtCYP20-2's levels were significantly lower in NDH mutants lacking a membrane domain, suggesting it plays a role in the assembly of NDH's hydrophobic section.
- However, the absence of AtCYP20-2 does not severely affect NDH function, indicating that other lumenal immunophilins can compensate for its role.
Article 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.
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| http://dx.doi.org/10.1016/j.febslet.2009.06.031 | DOI Listing |
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FEBS Lett
July 2009
Department of Biology, Plant Physiology and Molecular Biology, University of Turku, FI-20014 Turku, Finland.
Article Synopsis
- AtCYP20-2 is an immunophilin located in the thylakoid lumen, shown to assist the NAD(P)H dehydrogenase (NDH) due to its presence and co-migration with NDH in experiments.
- Studies indicate that AtCYP20-2's levels were significantly lower in NDH mutants lacking a membrane domain, suggesting it plays a role in the assembly of NDH's hydrophobic section.
- However, the absence of AtCYP20-2 does not severely affect NDH function, indicating that other lumenal immunophilins can compensate for its role.
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