Literature summary for 7.1.1.10 extracted from

Battchikova, N.; Wei, L.; Du, L.; Bersanini, L.; Aro, E.M.; Ma, W.
Identification of novel Ssl0352 protein (NdhS), essential for efficient operation of cyclic electron transport around photosystem I, in NADPH plastoquinone oxidoreductase (NDH-1) complexes of Synechocystis sp. PCC 6803 (2011), J. Biol. Chem., 286, 36992-37001 .

Search for more literature for 7.1.1.10

Cloned(Commentary)

Cloned (Comment)	Organism
gene ssl0352, recombinant expression of His6-tagged YFP-tagged wild-type and mutant subunits NdhS in Escherichia coli strain BL21(DE3)pLysS	Synechocystis sp. PCC 6803

Protein Variants

Protein Variants	Comment	Organism
additional information	screening of a transposon-tagged library of Synechocystis sp. 6803 cells grown under high light for subunit identification. Generation of mutantsx02ssl0352,x02ndhB (M55), Ssl0352-YFP-His6, and NdhM-YFP-His6 (two NDH-1-mediated CET (NDH-CET))-defective mutants are tagged in gene ssl0352. Construction of a ssl0352 deletion mutant and another mutant with Ssl0352 fused to yellow fluorescent protein (YFP) with a His6-tag are constructed. Immunoblotting, mass spectrometry, and confocal microscopy analyses reveal that the Ssl0352 protein resides in the thylakoid membrane and associates with the NDH-1L and NDH-1M complexes. Deletion of the ssl0352 gene considerably impairs the NDH-CET activity and also retards cell growth under high light conditions, indicating that NdhS is essential for efficient operation of NDH-CET. The high light-dependent phenotype of the two mutants results from defective NDH-CET. But the assembly of the NDH-1L and NDH-1M complexes and their content in the cells are not affected in the mutant	Synechocystis sp. PCC 6803

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
thylakoid membrane	His6-/YFP-tagged Ssl0352 protein/subunit NdhS resides in the thylakoid membrane and associates with the NDH-1L as well as the NDH-1M complexes	Synechocystis sp. PCC 6803	42651	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Synechocystis sp. PCC 6803

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1]	Synechocystis sp. PCC 6803	-	2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2]	-	?

Organism

Organism	UniProt	Comment	Textmining
Synechocystis sp. PCC 6803	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
native enzyme complex from membrane fraction of Synechocystis sp. PCC 6803 cells by ultracentrifugation at 150000 x g, isolation of thylakoid membranes. Recombinant His6-tagged YFP-tagged wild-type and mutant subunits NdhS from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography	Synechocystis sp. PCC 6803

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1]	-	Synechocystis sp. PCC 6803	2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2]	-	?

Synonyms

Synonyms	Comment	Organism
NADPH:plastoquinone oxidoreductase complex	-	Synechocystis sp. PCC 6803
NDH-1 complex	-	Synechocystis sp. PCC 6803

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7	-	assay at	Synechocystis sp. PCC 6803

Cofactor

Cofactor	Comment	Organism	Structure
Ferredoxin	-	Synechocystis sp. PCC 6803
plastoquinone	-	Synechocystis sp. PCC 6803

General Information

General Information	Comment	Organism
malfunction	deletion of gene ssl0352 impairs cyclic electron transfer (CET) but not the NDH-1 assembly. Deletion of the ssl0352 gene considerably impairs the NDH-CET activity and also retards cell growth under high light conditions, indicating that NdhS is essential for efficient operation of NDH-CET. The high light-dependent phenotype of the two mutants results from defective NDH-CET. But the assembly of the NDH-1L and NDH-1M complexes and their content in the cells are not affected in the mutant. No differences are observed in growth rates and photosynthetic O2 evolution between the wild-type and mutant DELTAssl0352	Synechocystis sp. PCC 6803
metabolism	cyanobacterial NADPH:plastoquinone oxidoreductase, or type I NAD(P)H dehydrogenase, or the NDH-1 complex is involved in plastoquinone reduction and cyclic electron transfer (CET) around photosystem I	Synechocystis sp. PCC 6803
physiological function	multisubunit NDH-1 complexes of cyanobacterial are involved in CO2 uptake and cyclic electron transfer (CET) around photosystem I. Protein Ssl0352 (UniProt ID P74795), is another NDH-1 subunit, termed NdhS, in Synechocystis sp. 6803 tightly associated with the NDH-1 complex. Subunit NdhS is important for the function of NDH-1 complexes. NdhS contains a Src homology 3-like domain and might be involved in interaction of the NDH-1 complex with an electron donor. CET produces extra ATP for cell metabolism particularly under stressful conditions. The Ssl0352 protein resides in the thylakoid membrane and associates with the NDH-1L and NDH-1M complexes	Synechocystis sp. PCC 6803

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Release 2023.1 (January 2023)