Mutants section of the slr1835 gene.
Genes and Mutants is a social mutants information repository. It allows biologist to submit a mutant information directly. This is a manual curated resource. You can contact the submitter by the e-mail address indicated.
MutantName indicates the mutant name.
GeneName indicates the gene name.
ProductName indicates the gene product name.
GeneticBackground indicates the genetic background: GT, Kazusa, PCC and etc...
DNA indicates the availability of the DNA material: yes or no.
DrugDirection indicates the direction of the drug marker: Fw (forward) or Rv (reverse).
DrugMarker indicates the construction of the drug maker.
AdditionalInformation indicates a free text of the mutant.
Post new mutant information of the slr1835 gene ... links to the submition form.
| Gene: psaB |
| Genes and Mutants | posted by Wim Vermaas <wim at asu.edu> at 1998-03-16 |
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| GeneName | psaB | | ProductName | PS I reaction center protein | | Function | PsaA and PsaB from the PS I reaction center heterodimer | | GeneticBackground | Not examined | | DNA | no | | Phenotype | yes | | PhenotypeDetails | Deletion of psaA and psaB leads to a light-sensitive phenotype.Mutants can be propagated at 5 umol photons/m2/s.Additional deletion of apcE leads to a less light-sensitive phenotype.Mutant characterization data indicate that in the absence of PS I, PS II-generated electrons flow to the cytochrome oxidase in the thylakoid; this oxidase may have a lower electron acceptance capacity than PS I, and overreduction of the PQ pool appears to be harmful to the cell:hence the light-sensitive phenotype of the psaAB- strain. | | AdditionalInformation | Shen, G., Boussiba, S., and Vermaas, W.F.J. (1993) Synechocystis sp. PCC 6803 strains lacking photosystem I and phycobilisome function. Plant Cell 5, 1853-1863.. Vermaas, W.F.J., Shen, G., and Styring, S. (1994) Electrons generated by photosystem II are utilized by an oxidase in the absence of photosystem I in the cyanobacterium Synechocystis sp. PCC 6803. FEBS Lett. 337, 103-108.. Vermaas, W.F.J. (1994) Molecular-genetic approaches to study photosynthetic and respiratory electron transport in thylakoids from cyanobacteria. Biochim. Biophys. Acta 1187, 181-186.. Wim Vermaas. Department of Plant Biology, and. Center for the Study of Early Events in Photosynthesis. Arizona State University. Box 871601. Tempe, AZ 85287-1601, USA. phone: (602)965-3698. fax: (602)965-6899 |
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| Mutant: BDK8 |
| Genes and Mutants | posted by Lee McIntosh <mcintos1 at pilot.msu.edu> at 1998-04-03 |
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| MutantName | BDK8 | | GeneName | psaB | | ProductName | Photosystem I P700 apoprotein subunit Ib | | Function | A subunit of PSI | | GeneticBackground | Not examined | | DNA | yes | | Phenotype | yes | | PhenotypeDetails | Unable to grow photoautotrophically. No PSI accumulation, while PSII assembled normally. Expression of the psaA gene was not affected by the mutation, but PsaA protein was not detected, indicating that stable PsaA homodimers did not form. | | AdditionalInformation | The BamHI-SphI fragment of the psaB gene was replaced by a kanamycin resistance cassette.. Reference: Genetic inactivation of the psaB gene in Synechocystis sp. PCC 6803 disrupts assembly of photosystem I. Lawrence B. Smart and Lee McIntosh. Plant Molecular Biology 21: 177-180, 1993.. Lee McIntosh. MSU-DOE Plant Research Laboratory. Michigan State University. East Lansing, MI 48824-1312 USA. Phone: (517) 353-7802. Fax: (517) 353-9168 | | Medline | 8425045 |
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| Mutant: C565S, C565H, C565D, L522V, L536M, L522V/L536M, L522P |
| Genes and Mutants | posted by Lee McIntosh <mcintos1 at pilot.msu.edu> at 1998-04-03 |
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| MutantName | C565S, C565H, C565D, L522V, L536M, L522V/L536M, L522P | | GeneName | psaB | | ProductName | Photosystem I P700 apoprotein subunit Ib | | Function | A subunit of PSI | | GeneticBackground | Not examined | | DNA | yes | | Phenotype | yes | | PhenotypeDetails | C565S, C565D, C565H, and L522P were unable to grow photoautotrophically and exhibited greatly reduced accumulation of PSI reaction-center proteins, indicating cystein 565 most likely does coordinate Fx, which is crucial for PSI biogenesis. C565S accumulated significantly more PSI than the other two cysteine mutants and displayed photoreduction of the [4Fe-4S] terminal electron acceptors FA and FB. Biophysical characterization of PSI complex containing C565S showed that a mixed-ligand [4Fe-4S] cluster in the Fx binding site was capable of electron transfer to FA and FB at a decreased quantum efficiency. | | AdditionalInformation | References:. 1. Mutational analysis of the structure and biogenesis of the photosystem I reaction center in the cyanobacterium Synechocystis sp. PCC 6803. Lawrence B. Smart, Patrick V. Warren, John H. Golbeck, and Lee McIntosh. Proc. Natl. Acad. Sci. USA 90: 1132-1136, 1993.. 2. Site-directed conversion of cysteine-565 to serine in PsaB of photosystem I results in the assembly of [3Fe-4S] and [4Fe-4S] clusters in Fx. A mixed-ligand [4Fe-4S] cluster is capable of electron transfer to FA and FB. Patrick V. Warren, Lawrence B. Smart, Lee McIntosh, and John H. Golbeck. Biochemistry 32(16): 4411-4419, 1993.. 3. A mixed-ligand iron-sulfur cluster (C556SPsaB or C565SPsaB) in the Fx-binding site leads to a decreased quantum efficiency of electron transfer in photosystem I. Vassiliev IR, Jung YS, Smart LB, Schulz R, McIntosh L, Golbeck JH. Biophysical Journal 69(4): 1544-1553, 1995.. . Lee McIntosh. MSU-DOE Plant Research Laboratory. Michigan State University. East Lansing, MI 48824-1312 USA. Phone: (517) 353-7802. Fax: (517) 353-9168 | | Medline | 8534825, 8386546 |
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| Mutant: R561E, W570Q, D566A, D566K, D577A, D577K, C556S, F554A, K547E, Delta-L522 |
| Genes and Mutants | posted by Lee McIntosh <mcintos1 at pilot.msu.edu> at 1998-04-04 |
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| MutantName | R561E, W570Q, D566A, D566K, D577A, D577K, C556S, F554A, K547E, Delta-L522 | | GeneName | psaB | | ProductName | Photosystem I P700 apoprotein subunit Ib | | Function | A subunit of PSI | | GeneticBackground | Not examined | | DNA | yes | | Phenotype | yes | | PhenotypeDetails | R561E, C556S, and Delta-L522 were unable to grow photoautotrophically. They had greatly reduced levels of PSI accumulation. Biophysical characterization of PSI complex containing C556S showed that a mixed-ligand [4Fe-4S] cluster in the Fx binding site was capable of electron transfer to FA and FB at a decreased quantum efficiency. | | AdditionalInformation | R561 residue was proposed to be involved in PsaC binding and is indeed involved in electrostatics and PSI stability. C556 is a ligand to Fx cluster. L522 is part of proposed leucine zipper.. References:. 1. A new set of site-directed mutations in photosystem I core reaction center from Synechocystis sp. PCC 6803. Schulz R., Smart L.B., Yu J., and McIntosh L. In Photosynthesis: from light to biosphere Vol.II, Paul Mathis, editor. 119-122, 1995.. 2. Structure-function studies on the interaction of PsaC with the photosystem I heterodimer. Rodday, S.M., Schulz, R., McIntosh, L., and Biggins, J. (1994) Photosynth. Res. 42, 185-190.. . Lee McIntosh. MSU-DOE Plant Research Laboratory. Michigan State University. East Lansing, MI 48824-1312 USA. Phone: (517) 353-7802. Fax: (517) 353-9168 | | Medline | 8534825 |
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