A1 Refereed original research article in a scientific journal

Identification of NdhL and Ssl1690 (NdhO) in NDH-1L, and NDH-1M complexes of Synechocystis sp PCC 6803




AuthorsBattchikova N, Zhang PP, Rudd S, Ogawa T, Aro EM

PublisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC

Publication year2005

Journal:Journal of Biological Chemistry

Journal name in sourceJOURNAL OF BIOLOGICAL CHEMISTRY

Journal acronymJ BIOL CHEM

Volume280

Issue4

First page 2587

Last page2595

Number of pages9

ISSN0021-9258

DOIhttps://doi.org/10.1074/jbc.M410914200


Abstract
The subunit compositions of two types of NAD(P)H dehydrogenase complexes of Synechocystis sp. PCC 6803, NDH-1L and NDH-1M, were studied by two-dimensional blue-native/SDS-PAGE followed by electrospray tandem mass spectrometry. Fifteen proteins were observed in NDH-1L including hydrophilic subunits (NdhH, -K, -I, -J, -M, and -N) and hydrophobic subunits (NdhA, -B, -E, -G, -D1, and -F1). In addition, NdhL and a novel subunit, SsI1690 (designated NdhO), were shown to be components of this complex. All subunits mentioned above were present in the NDH-1M complex except NdhD1 and NdhF1. NdhL and SsI1690 (NdhO) were homologous to hypothetical proteins encoded by genomic DNA in higher plants, suggesting that chloroplast NDH-1 complexes contain related subunits. Diagnostic sequence motifs were found for both NdhL and NdhO homologous proteins. Analysis of ndhL deletion mutant (W revealed the presence of assembled NDH-1L and NDH-1M complexes, but these complexes appear to be functionally impaired in the absence of NdhL. Both NDH-1 complexes were absent in the ndhB deletion mutant (M55).



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