Different and rapid responses of four cyanobacterial psbA transcripts to changes in light intensity

Bustos, Silvia A.; Schaefer, Michael; Golden, Susan S.

doi:10.1128/jb.172.4.1998-2004.1990

Cited by 113 publications

(80 citation statements)

References 20 publications

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“…These results show that proteins binding to psbDII DNA do not interact efficiently with the psbDl DNA fragment but bind strongly to the upstream region of the psbAII gene. The psbAII gene encodes the Dl protein, the other member of the photosystem II reaction center, and is also induced by a shift to high light intensity (7).…”

Section: Resultsmentioning

confidence: 99%

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Expression of the psbDII gene in Synechococcus sp. strain PCC 7942 requires sequences downstream of the transcription start site

1991

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The psbDI and psbDII genes in Synechococcus sp. strain PCC 7942 encode the D2 polypeptide, an essential component of the photosystem II reaction center. Previous studies have demonstrated that transcripts from psbDII, but not psbDI, increase in response to high light intensity. Soluble proteins from Synechococcus cells shifted to high light were found to have affinity for DNA sequences upstream from the psbDII coding region. DNA mobility-shift and copper-phenanthroline footprinting assays of a 258-bp fragment revealed three distinct DNA-protein complexes that mapped to the untranslated leader region between +11 and +84. Deletion of the upstream flanking region to -42 had no effect on the expression of a psbDII-lacZ reporter gene or its induction by light, whereas a promoterless construct supported only minimal background levels of I8-galactosidase. A 4-bp deletion within the first protected region of the footprint decreased the 0-galactosid4se activity to approximately 2% of that of the undeleted control, but gene expression remained responsive to light. Deletion of the three protected regions completely abolished both gene expression and light induction. These results suggest that the psbDII gene requires elements within the untranslated leader region for efficient gene expression, one of which may be involved in regulation by light.Cyanobacteria make up a large and diverse group of photosynthetic bacteria. They share with plants the ability to use two photosynthetic reaction centers linked in series, termed photosystems I and II, to reduce photooxidized chlorophyll with electrons obtained from water, releasing molecular oxygen as a by-product. Components of the photosynthetic apparatus of cyanobacteria are highly conserved with their counterparts in the chloroplasts of higher plants (4). The reaction center core of photosystem II contains a dimer of two structurally similar proteins, Dl and D2 (48), which are encoded by the psbA and psbD genes, respectively (4). Dl and D2 house the photoreactive chlorophyll, primary acceptor, and other cofactors involved in electron transport through photosystem II (25,33,48). Both psbA and psbD are unique genes in the chloroplast genomes of most plants (19,36,41,53) but are present in more than one copy in cyanobacterial genomes (9,15,18

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Section: Resultsmentioning

confidence: 99%

“…DNA mobility-shift assays of the wild-type probe 2 fragment and DNA fragments deleted for one or more of the binding sites. All DNA probes were incubated with heparin-Sepharose column fraction 7 (Fig. 2B, lane 7).…”

Section: Resultsmentioning

confidence: 99%

Expression of the psbDII gene in Synechococcus sp. strain PCC 7942 requires sequences downstream of the transcription start site

1991

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“…The ATDC protein is implicated in the human genetic disease ataxia-telangiectasia. In addition, an open reading frame (ORF) encoding a cyanobacterial PKCI-1 homologue has been identified, and inactivation of this ORF in cyanobacteria results in a slow growth phenotype for this organism (8). These results suggest a possible role for PKCI-1 in signal transduction pathways.…”

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confidence: 85%

Three-dimensional structure of human protein kinase C interacting protein 1, a member of the HIT family of proteins.

Lima

Klein²,

Weinstein³

et al. 1996

Proc. Natl. Acad. Sci. U.S.A.

103

109

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The three-dimensional structure of protein kinase C interacting protein 1 (PKCI-1) has been solved to high resolution by x-ray crystallography using single isomorphous replacement with anomalous scattering. The gene encoding human PKCI-1 was cloned from a cDNA library by using a partial sequence obtained from interactions identified in the yeast two-hybrid system between PKCI-1 and the regulatory domain of protein kinase C-f3. The PKCI-1 protein was expressed in Pichia pastoris as a dimer of two 13.7-kDa polypeptides. PKCI-1 is a member of the HIT family of proteins, shown by sequence identity to be conserved in a broad range of organisms including mycoplasma, plants, and humans. Despite the ubiquity of this protein sequence in nature, no distinct function has been shown for the protein product in vitro or in vivo. The PKCI-1 protomer has an cx+f3 meander fold containing a five-stranded antiparallel sheet and two helices. Two protomers come together to form a 10-stranded antiparallel sheet with extensive contacts between a helix and carboxy terminal amino acids of a protomer with the corresponding amino acids in the other protomer. PKCI-1 has been shown to interact specifically with zinc. The three-dimensional structure has been solved in the presence and absence of zinc and in two crystal forms. The structure of human PKCI-1 provides a model of this family of proteins which suggests a stable fold conserved throughout nature.

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“…hinT Is Required for Growth under High Salt ConditionsEarlier a Synechococcus strain was constructed in which the Hint-homologous gene was deleted and a slow growth phenotype was reported (37). Using the BB3 strain, we constructed a stain with an E. coli hinT disruption and carried out a screen for mutant phenotypes.…”

Section: Nucleoside and Leaving Group Specificity Of Bacterial Andmentioning

confidence: 99%

31P NMR and Genetic Analysis Establish hinT as the Only Escherchia coli Purine Nucleoside Phosphoramidase and as Essential for Growth under High Salt Conditions

Chou

Bieganowski

Shilinski

et al. 2005

Journal of Biological Chemistry

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Eukaryotic cells encode AMP-lysine (AMP-N-⑀-(N-␣acetyl lysine methyl ester) 5-phosphoramidate) hydrolases related to the rabbit histidine triad nucleotidebinding protein 1 (Hint1) sequence. Bacterial and archaeal cells have Hint homologs annotated in a variety of ways, but the enzymes have not been characterized, nor have phenotypes been described due to loss of enzymatic activity. We developed a quantitative 31 P NMR assay to determine whether Escherichia coli possesses an adenosine phosphoramidase activity. Indeed, soluble lysates prepared from wild-type laboratory E. coli exhibited activity on the model substrate adenosine 5-monophosphoramidate (AMP-NH 2 ). The E. coli Hint homolog, which had been comprehensively designated ycfF and is here named hinT, was cloned, overexpressed, purified, and characterized with respect to purine nucleoside phosphoramidate substrates. Bacterial hinT was several times more active than human or rabbit Hint1 on five model substrates. In addition, bacterial and mammalian enzymes preferred guanosine versus adenosine phosphoramidates as substrates. Analysis of the lysates from a constructed hinT knock-out strain of E. coli demonstrated that all of the cellular purine nucleoside phosphoramidase activity is due to hinT. Physiological analysis of this mutant revealed that the loss of hinT results in failure to grow in media containing 0.75 M KCl, 0.9 M NaCl, 0.5 M NaOAc, or 10 mM MnCl 2 . Thus, cation-resistant bacterial cell growth may be dependent on the hydrolysis of adenylylated and/or guanylylated phosphoramidate substrates by hinT.

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Different and rapid responses of four cyanobacterial psbA transcripts to changes in light intensity

Cited by 113 publications

References 20 publications

Expression of the psbDII gene in Synechococcus sp. strain PCC 7942 requires sequences downstream of the transcription start site

Expression of the psbDII gene in Synechococcus sp. strain PCC 7942 requires sequences downstream of the transcription start site

Three-dimensional structure of human protein kinase C interacting protein 1, a member of the HIT family of proteins.

31P NMR and Genetic Analysis Establish hinT as the Only Escherchia coli Purine Nucleoside Phosphoramidase and as Essential for Growth under High Salt Conditions

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