Nucleotide sequence of a wheat chloroplast gene encoding the proteolytic subunit of an ATP-dependent protease

Gray, John C.; Hird, Sean M.; Dyer, Tristan A.

doi:10.1007/bf00039435

Cited by 60 publications

(21 citation statements)

References 20 publications

(18 reference statements)

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“…Results presented in this work indicate that chloroplasts contain a protein similar to a cyanobacterial Ca2+-stimulated protease (Lockau et al, 1988) and a protein similar to the bacterial clpP gene product. The clpP gene is found in the chloroplast genome (Ohyama et al, 1986;Shinozaki et al, 1986;Hiratsuka et al, 1989;Gray et al, 1990;Maurizi et al, 1990;Clarke et al, 1994) and is expressed, and the corresponding protein accumulates. Both proteases are expressed in leaves and not in roots, but their expression is differentially affected by light.…”

Section: Discussionmentioning

confidence: 99%

“…However, there is good genetic evidence for the existence of at least one such protease. An ORF in the chloroplast genome (Shinozaki et al, 1986;Ohyama et al, 1986;Hiratsuka et al, 1989) shows high similarity to ClpP, the proteolytic subunit of the Escherichia coli Clp protease (Gray et al, 1990;h4aurizi et al, 1990;Clarke et al, 1994). A protein similar to a regulatory subunit of Clp protease has also been found in plants.…”

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confidence: 99%

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Immunological Detection of Proteins Similar to Bacterial Proteases in Higher Plant Chloroplasts

Ostersetzer

Tabak

Yarden

et al. 1996

European Journal of Biochemistry

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Despite numerous demonstrations of protein degradation in chloroplasts of higher plants, little is known about the identity of the proteases involved in these reactions. To identify chloroplast proteases by immunological means, we investigated two proteins: ClpP, a protein similar to the proteolytic subunit of the bacterial ATP‐dependent Clp protease, for which a gene is found in the chloroplast genome [Maurizi, M. R., Clark, W. P., Kim, S. H. & Gottesman, S. (1990) J. Biol. Chem. 265, 12546–12552] and PrcA, a cyanobacterial Ca2+‐stimulated protease [Maldener, I., Lockau, W., Cai, Y. & Wolk, P. (1991) Mol. & Gen. Genet. 225, 113–120]. We expressed the clpP gene from rice in Escherichia coli, purified its product, and generated antibodies against the product. Western blot analysis revealed the ClpP protein in different leaf extracts. Analysis of fractionated barley chloroplasts revealed that the protein was associated with the stromal fraction. The expression of ClpP is light independent and tissue specific, as it was found in green and etiolated barley leaves, but not in roots. A second protein, similar to the cyanobacterial protease PrcA, was also detected in chloroplasts. Antibody against this protease recognized proteins in various leaf extracts. When pea chloroplasts were fractionated, the antibody only recognized a stromal protein. The expression of this protein is regulated by light, as it was found in green leaves but not in etiolated leaves. The tissue specificity of PrcA was similar to that of ClpP in that it could not be detected in root extracts.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Immunological Detection of Proteins Similar to Bacterial Proteases in Higher Plant Chloroplasts

Ostersetzer

Tabak

Yarden

et al. 1996

European Journal of Biochemistry

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“…qRT-PCR amplifications were performed on RNA extracted from 4-and 12-d-old seedlings and 21-d-old rosettes of Col-0 and the sca3-2 mutant (Table I) to quantify expression of the following plastid genes: clpP (assumed to be class II), rpoB, rpoC1, accD (assumed to be class III), and rps18 (not classified, given that its transcription initiation sites and promoters have not been mapped). These genes respectively encode the proteolytic subunit of the Clp ATP-dependent protease (Gray et al, 1990;Maurizi et al, 1990), the plastid b (Hu and Bogorad, 1990) and b# core subunits of PEP (Shinozaki et al, 1986), a subunit of the acetyl-CoA carboxylase involved in lipid biosynthesis (Sasaki et al, 1993), and a ribosomal protein (Shinozaki et al, 1986).…”

Section: Effects Of Sca3 Mutations On Expression Of Plastid Genesmentioning

confidence: 99%

The SCABRA3 Nuclear Gene Encodes the Plastid RpoTp RNA Polymerase, Which Is Required for Chloroplast Biogenesis and Mesophyll Cell Proliferation in Arabidopsis

2006

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In many plant species, a subset of the genes of the chloroplast genome is transcribed by RpoTp, a nuclear-encoded plastidtargeted RNA polymerase. Here, we describe the positional cloning of the SCABRA3 (SCA3) gene, which was found to encode RpoTp in Arabidopsis (Arabidopsis thaliana). We studied one weak (sca3-1) and two strong (sca3-2 and sca3-3) alleles of the SCA3 gene, the latter two showing severely impaired plant growth and reduced pigmentation of the cotyledons, leaves, stem, and sepals, all of which were pale green. The leaf surface was extremely crumpled in the sca3 mutants, although epidermal cell size and morphology were not perturbed, whereas the mesophyll cells were less densely packed and more irregular in shape than in the wild type. A significant reduction in the size, morphology, and number of chloroplasts was observed in homozygous sca3-2 individuals whose photoautotrophic growth was consequently perturbed. Microarray analysis showed that several hundred nuclear genes were differentially expressed in sca3-2 and the wild type, about one-fourth of which encoded chloroplast-targeted proteins. Quantitative reverse transcription-PCR analyses showed that the sca3-2 mutation alters the expression of the rpoB, rpoC1, clpP, and accD plastid genes and the SCA3 paralogs RpoTm and RpoTmp, which respectively encode nuclear-encoded mitochondrion or dually targeted RNA polymerases. Double-mutant analysis indicated that RpoTmp and SCA3 play redundant functions in plant development. Our findings support a role for plastids in leaf morphogenesis and indicate that RpoTp is required for mesophyll cell proliferation.

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“…In photosynthesis, the development is manifested by the large number of studies on the proteolytic degradation of the D1 protein during repair of photoinactivated PSI1 reaction centres (Prasil et al, 1992;Aro et al, 1993) Moreover, the recent discovery of the presence of a clp-protease (Goldberg, 1992) in the chloroplast has further added to this interest (Gray, 1990;Moore and Keegstra, 1993). In this study, we have discovered a proteolytic activity involved in the removal of LHCII under conditions of elevated irradiance of spinach leaves.…”

Section: Discussionmentioning

confidence: 69%

Regulatory Proteolysis of the Major Light‐Harvesting Chlorophyll a/b Protein of Photosystem II by a Light‐Induced Membrane‐Associated Enzymic System

Lindahl

Yang

Andersson

1995

European Journal of Biochemistry

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An endogenous proteolytic activity associated with spinach chloroplast thylakoid membranes has been identified. This enzymic activity is involved in the degradation of the major light-harvesting chlorophyll alb protein of photosystem I1 (LHCII) in response to exposure of leaves to increased irradiance. This proteolysis of LHCII requires an induction period and can only be detected 48-72 hours after transfer of the plants from low-intensity to high-intensity light. Once initiated by high-intensity light, the degradation of LHCII can readily occur in complete darkness. The proteolysis can, after induction in vivo, be experimentally followed in vitro, both in isolated intact chloroplasts and thylakoid membranes. The proteolytic process is strictly dependent on ATP and the protease involved is of the serine or cysteine type. The activity can be released from isolated thylakoid membranes by washing with high concentrations of NaCl and reconstituted by readdition of the desalted wash supernatant. It is concluded that the protease is extrinsically bound to the outer surface of the stroma-exposed regions of the stacked thylakoid membrane. The mechanism for the induction of the proteolytic process as well as its relation to previously described thylakoid proteases will be discussed.

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Nucleotide sequence of a wheat chloroplast gene encoding the proteolytic subunit of an ATP-dependent protease

Cited by 60 publications

References 20 publications

Immunological Detection of Proteins Similar to Bacterial Proteases in Higher Plant Chloroplasts

Immunological Detection of Proteins Similar to Bacterial Proteases in Higher Plant Chloroplasts

The SCABRA3 Nuclear Gene Encodes the Plastid RpoTp RNA Polymerase, Which Is Required for Chloroplast Biogenesis and Mesophyll Cell Proliferation in Arabidopsis

Regulatory Proteolysis of the Major Light‐Harvesting Chlorophyll a/b Protein of Photosystem II by a Light‐Induced Membrane‐Associated Enzymic System

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