RbcX Can Function as a Rubisco Chaperonin, But is Non-Essential in Synechococcus PCC7942

Abstract The functional location of carotenoids in the photosynthetic apparatus of -crtB and -pys transformants of the cyanobacterium Synechococcus PCC7942 was studied and compared with a control strain -pFP 1-3. These transformants overproduce carotenoids due to the insertion of an additional foreign phytoene synthase gene. A higher carotenoid content was found for -crtB and -pys transformants both in whole cells and isolated membranes; the -crtB transformant was also enriched with chlorophyll. 77-K fluorescence emission and excitation spectra of the phycobilin-free membranes were examined for a possible location of overproduced carotenoids in pigment-protein complexes in situ. A similar ratio of the amplitudes of fluorescence bands at 716 and 695 nm emitted by photosystems I and II, found for the three strains, indicates that the stoichiometry between photosystems of the transformants was not changed. Overproduced carotenoids are not located in the core antenna of photosys tem I, since 77-K fluorescence excitation spectra for photosystem I of isolated membranes from the studied strains do not differ in the region of carotenoid absorption. When illuminated with light of the same intensity but different quality, absorbed preferentially by either carotenoids, chlorophylls or phycobilins, respectively, oxygen evolution was found always higher in the transformants -crtB and -pys than in -pFP 1-3 control cells. Identical kinetics of fluorescence induction of all strains under carotenoid excitation did not reveal a higher activity of photosystem II in cells enriched with carotenoids. It is suggested that overproduced carotenoids of the transformants are not involved in photosynthetic light-harvesting; rather they may serve to protect the cells and its membranes against photodestruction.

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Accumulation of ß-carotene in the Cyanobacteriurn Synechococcus PCC7942 under Low Concentrations of Herbicide Norflurazon

Research in Photosynthesis ◽

10.1007/978-94-009-0383-8_6 ◽

1992 ◽

pp. 35-38

Author(s):

Kazumori Masamoto

Keyword(s):

Low Concentrations ◽

Synechococcus Pcc7942

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Carboxysome genomics: a status report

Functional Plant Biology ◽

10.1071/pp01200 ◽

2002 ◽

Vol 29 (3) ◽

pp. 175 ◽

Cited By ~ 42

Author(s):

Gordon C. Cannon ◽

Sabine Heinhorst ◽

Christopher E. Bradburne ◽

Jessup M. Shively

Keyword(s):

Status Report ◽

Thiobacillus Denitrificans ◽

Nostoc Punctiforme ◽

Sequence Identity ◽

Putative Operon ◽

Multiple Copies ◽

Synechococcus Pcc7942 ◽

Halothiobacillus Neapolitanus ◽

Fixation Of Carbon Dioxide ◽

Synechocystis Sp

Carboxysomes, microcompartments that enhance the fixation of carbon dioxide by Rubisco, are found in several chemoautotrophs and in all cyanobacteria thus far examined. The genes for Rubisco large (cbbL) and small (cbbS) subunits (cbb for Calvin-Benson-Bassham), along with the genes (csoS) for the carboxysome shell peptides, are organized in a putative operon in Halothiobacillus neapolitanus in the following order: cbbL,cbbS, csoS2, csoS3, orfA, orfB, csoS1C, csoS1A, and csoS1B. DNA sequencing has revealed essentially the same operon in three other thiobacilli, Acidithiobacillus ferrooxidans, Thiomonas intermedia, and Thiobacillus denitrificans. The carboxysome genes are also clustered inSynechococcus sp. and Synechocystis sp., although in some cases certain genes lie outside the cluster. The genes, labelled ccm for CO2 concentrating mechanism, exist in Synechococcus PCC7942 in the order ccmK, ccmL, ccmM, ccmN, and ccmO, and are located upstream of the Rubisco genes. ccmO is absent, and multiple copies of ccmK exist in some species. The ccmK/ccmO and ccmL genes are homologues of csoS1CAB andorfAB, respectively. The ccmM and ccmN genes have no apparent counterpart in the thiobacilli. More recently, the genome sequence of four additional cyanobacteria has become available. The carboxysome genes in Nostoc punctiforme are clustered like, and are similar to, the genes of the earlier mentioned cyanobacteria. However, the three marine organisms Prochlorococcus marinus MIT9313, P. marinus MED4, and Synechococcus WH8102, possess an operon nearly identical to that found in thiobacilli. Furthermore, the genes exhibit surprising sequence identity to the carboxysome genes of the thiobacilli.

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