A cAMP Receptor Protein, SYCRP1, is Responsible for the Cell Motility of Synechocystis sp. PCC 6803

Yoshimura, Hidehisa; Yoshihara, Shizue; Okamoto, Shinobu; Ikeuchi, Masahiko; Ohmori, Masayuki

doi:10.1093/pcp/pcf050

Cited by 44 publications

(55 citation statements)

References 21 publications

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“…Southern blotting further confirmed that recombination had occurred specifically in the sycrp1 locus and that sll1924 (sycrp2) or slr0593 homologues were not disrupted (data not shown). Additional evidence for gene inactivation was obtained by observing phototactic and crp nonmotile phenotypes (Yoshimura et al, 2002b) (data not shown). To discount polar effects of genes surrounding the site of sycrp1 inactivation, transcript abundance of the two genes flanking sycrp1 (sll1370 and sll1372) was quantified in photoautotrophically growing cultures by RT-QPCR.…”

Section: Crp Sequence-specific Binding Was Demonstratedmentioning

confidence: 71%

Illumination stimulates cAMP receptor protein-dependent transcriptional activation from regulatory regions containing class I and class II promoter elements in Synechocystis sp. PCC 6803

et al. 2009

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The cAMP receptor protein (Crp) is a global transcriptional regulator that binds sequence-specific promoter elements when associated with cAMP. In the motile cyanobacterium Synechocystis sp. strain PCC 6803, intracellular cAMP increases when dark-adapted cells are illuminated. Previous work has established that Crp binds proposed Crp target sites upstream of slr1351 (murF), sll1874 (chlA II ), sll1708 (narL), slr0442 and sll1268 in vitro, and that slr0442 is downregulated in a crp mutant during photoautotrophic growth. To identify additional Crp target genes in Synechocystis, 11 different Crp binding sites proposed during a previous computational survey were tested for in vitro sequence-specific binding and crp-dependent transcription. The results indicate that murF, chlA II and slr0442 can be added as 'target genes of Sycrp1' in Synechocystis. Promoter mapping of the targets revealed the same close association of RNA polymerase and Crp as that found in Escherichia coli class I and class II Crp-regulated promoters, thereby strongly suggesting similar mechanisms of transcriptional activation.

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Section: Crp Sequence-specific Binding Was Demonstratedmentioning

confidence: 71%

Illumination stimulates cAMP receptor protein-dependent transcriptional activation from regulatory regions containing class I and class II promoter elements in Synechocystis sp. PCC 6803

et al. 2009

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“…These fibrous extensions may be elongated stretches of outer wall layers. They are more coarse than fimbriae (28) but could be related to some of the coarser pili observed in Synechocystis strain PCC 6803 (2,32). Negatively stained images of whole mounts of fixed cells did not reveal pili on either WT or mutants, which does not rule out their presence.…”

Section: Sll1556 and Ipp Isomerase Activity In Vitromentioning

confidence: 99%

Inactivation ofsll1556inSynechocystisStrain PCC 6803 Impairs Isoprenoid Biosynthesis from Pentose Phosphate Cycle Substrates In Vitro

et al. 2004

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In cyanobacteria many compounds, including chlorophylls, carotenoids, and hopanoids, are synthesized from the isoprenoid precursors isopentenyl diphosphate (IPP) and dimethylallyl diphosphate. Isoprenoid biosynthesis in extracts of the cyanobacterium Synechocystis strain PCC 6803 grown under photosynthetic conditions, stimulated by pentose phosphate cycle substrates, does not appear to require methylerythritol phosphate pathway intermediates. The sll1556 gene, distantly related to type 2 IPP isomerase genes, was disrupted by insertion of a Kan r cassette. The mutant was fully viable under photosynthetic conditions although impaired in the utilization of pentose phosphate cycle substrates. Compared to the parental strain the ⌬sll1556 mutant (i) is deficient in isoprenoid biosynthesis in vitro with substrates including glyceraldehyde-3-phosphate, fructose-6-phosphate, and glucose-6-phosphate; (ii) has smaller cells (diameter ca. 13% less); (iii) has fewer thylakoids (ca. 30% less); and (iv) has a more extensive fibrous outer wall layer. Isoprenoid biosynthesis is restored with pentose phosphate cycle substrates plus the recombinant Sll1556 protein in the ⌬sll1556 supernatant fraction. IPP isomerase activity could not be demonstrated for the purified Sll1556 protein under our in vitro conditions. The reduction of thylakoid area and the effect on outer wall layer components are consistent with an impairment of isoprenoid biosynthesis in the mutant, possibly via hopanoid biosynthesis. Our findings are consistent with an alternate metabolic shunt for biosynthesis of isoprenoids.Isoprenoids are required for many cell processes including photosynthesis, membrane stability, electron transport, and the cellular production of carotenoids, rubber, and fragrances. More than 30,000 isoprenoid compounds have been described. Synthesis of the essential 5-carbon building blocks of isoprenoids, isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), can be attributed to one of two pathways. The mevalonic acid pathway, the sole pathway in animals and in many bacteria, also occurs in the cytoplasm of plant cells, where it is responsible for synthesis of sterols and ubiquinones (18,20). The 2-C-methyl-D-erythritol-4-phosphate (MEP) pathway occurs in Escherichia coli and many other bacteria as well as in cyanobacteria. It is also present in chloroplasts, where it provides substrates for the synthesis of carotenoids, chlorophylls, and quinones. This pathway is believed important for cyanobacterial photosynthetic pigment biosynthesis including that of carotenoids and the phytolation of chlorophyll and in hopanoid synthesis of bacterial and cyanobacterial cell walls and membranes (8,20,24). Most of the MEP pathway genes have been functionally verified in the gram-negative heterotrophic bacterium E. coli (reviewed in references 4, 14, 18, and 20), and this bacterium has thus become the standard for defining the MEP pathway in other organisms. The MEP pathway is typically represented as a linear sequence of reactions commenci...

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“…In Synechocystis sp. inactivation of CRP (sycrp1, sll1371) resulted in an apparently nonmotile phenotype (27,28).…”

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confidence: 99%

Phototaxis and Impaired Motility in Adenylyl Cyclase and Cyclase Receptor Protein Mutants ofSynechocystissp. Strain PCC 6803

et al. 2006

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We have carefully characterized and reexamined the motility and phototactic responses of Synechocystis sp. adenylyl cyclase (Cya1) and catabolite activator protein (SYCRP1) mutants to different light regimens, glucose, 3-(3,4-dichlorophenyl)-1,1-dimethylurea, and cyclic AMP. We find that contrary to earlier reports, cya1 and sycrp1 mutants are motile and phototactic but are impaired in one particular phase of phototaxis in comparison with wild-type Synechocystis sp.

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A cAMP Receptor Protein, SYCRP1, is Responsible for the Cell Motility of Synechocystis sp. PCC 6803

Cited by 44 publications

References 21 publications

Illumination stimulates cAMP receptor protein-dependent transcriptional activation from regulatory regions containing class I and class II promoter elements in Synechocystis sp. PCC 6803

Illumination stimulates cAMP receptor protein-dependent transcriptional activation from regulatory regions containing class I and class II promoter elements in Synechocystis sp. PCC 6803

Inactivation ofsll1556inSynechocystisStrain PCC 6803 Impairs Isoprenoid Biosynthesis from Pentose Phosphate Cycle Substrates In Vitro

Phototaxis and Impaired Motility in Adenylyl Cyclase and Cyclase Receptor Protein Mutants ofSynechocystissp. Strain PCC 6803

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