TY - JOUR
T1 - A novel redoxin in the thylakoid membrane regulates the titer of photosystem I
AU - Zhu, Yuehui
AU - Liberton, Michelle
AU - Pakrasi, Himadri B.
N1 - Publisher Copyright:
© 2016 by The American Society for Biochemistry and Molecular Biology, Inc.
PY - 2016/9/2
Y1 - 2016/9/2
N2 - In photosynthetic organisms like cyanobacteria and plants, the main engines of oxygenic photosynthesis are the pigmentprotein complexes photosystem I (PSI) and photosystem II (PSII) located in the thylakoid membrane. In the cyanobacterium Synechocystis sp. PCC 6803, the slr1796 gene encodes a single cysteine thioredoxin-like protein, orthologs of which are found in multiple cyanobacterial strains as well as chloroplasts of higher plants. Targeted inactivation of slr1796 in Synechocystis 6803 resulted in compromised photoautotrophic growth. The mutant displayed decreased chlorophyll a content. These changes correlated with a decrease in the PSI titer of the mutant cells, whereas the PSII content was unaffected. In the mutant, the transcript levels of genes for PSI structural and accessory proteins remained unaffected, whereas the levels of PSI structural proteins were severely diminished, indicating that Slr1796 acts at a posttranscriptional level. Biochemical analysis indicated that Slr1796 is an integral thylakoid membrane protein. We conclude that Slr1796 is a novel regulatory factor that modulates PSI titer.
AB - In photosynthetic organisms like cyanobacteria and plants, the main engines of oxygenic photosynthesis are the pigmentprotein complexes photosystem I (PSI) and photosystem II (PSII) located in the thylakoid membrane. In the cyanobacterium Synechocystis sp. PCC 6803, the slr1796 gene encodes a single cysteine thioredoxin-like protein, orthologs of which are found in multiple cyanobacterial strains as well as chloroplasts of higher plants. Targeted inactivation of slr1796 in Synechocystis 6803 resulted in compromised photoautotrophic growth. The mutant displayed decreased chlorophyll a content. These changes correlated with a decrease in the PSI titer of the mutant cells, whereas the PSII content was unaffected. In the mutant, the transcript levels of genes for PSI structural and accessory proteins remained unaffected, whereas the levels of PSI structural proteins were severely diminished, indicating that Slr1796 acts at a posttranscriptional level. Biochemical analysis indicated that Slr1796 is an integral thylakoid membrane protein. We conclude that Slr1796 is a novel regulatory factor that modulates PSI titer.
UR - http://www.scopus.com/inward/record.url?scp=84984917681&partnerID=8YFLogxK
U2 - 10.1074/jbc.M116.721175
DO - 10.1074/jbc.M116.721175
M3 - Article
C2 - 27382055
AN - SCOPUS:84984917681
SN - 0021-9258
VL - 291
SP - 18689
EP - 18699
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 36
ER -