An
            <i>Arabidopsis</i>
            Mutant Defective in the Plastid General Protein Import Apparatus

Jarvis, Paul; Chen, Lih Jen; Li, Hsou Min; Peto, Charles A.; Fankhauser, Christian; Chory, Joanne

doi:10.1126/science.282.5386.100

Cited by 317 publications

(459 citation statements)

References 24 publications

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“…The +/tic110-1, hsp93-V-1, tic40-4, ppi1-1 and hsp93-V-1 hsp93-III-1 (hsp93-V/III) mutants employed to derive the calibration relationships have all been described previously (Jarvis et al 1998;Kovacheva et al 2005;Kovacheva et al 2007). Similarly, the pph-1 and pao1 mutants have been presented in earlier reports (Pruzinska et al 2005;Schelbert et al 2009).…”

Section: Plant Materials and Growth Conditionsmentioning

confidence: 95%

Use of a SPAD-502 meter to measure leaf chlorophyll concentration in Arabidopsis thaliana

2010

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The SPAD-502 meter is a hand-held device that is widely used for the rapid, accurate and non-destructive measurement of leaf chlorophyll concentrations. It has been employed extensively in both research and agricultural applications, with a range of different plant species. However, its utility has not been fully exploited in relation to the most intensively studied model organism for plant science research, Arabidopsis thaliana. Measurements with the SPAD-502 meter produce relative SPAD meter values that are proportional to the amount of chlorophyll present in the leaf. In order to convert these values into absolute units of chlorophyll concentration, calibration curves must be derived and utilized. Here, we present calibration equations for Arabidopsis that can be used to convert SPAD values into total chlorophyll per unit leaf area (nmol/cm 2 ; R 2 = 0.9960) or per unit fresh weight of leaf tissue (nmol/mg; R 2 = 0.9809). These relationships were derived using a series of Arabidopsis chloroplast biogenesis mutants that exhibit chlorophyll deficiencies of varying severity, and were verified by the subsequent analysis of senescent or light-stressed leaves. Our results revealed that the converted SPAD values differ from photometric measurements of solventextracted chlorophyll by just ~6% on average.

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Section: Plant Materials and Growth Conditionsmentioning

confidence: 95%

Use of a SPAD-502 meter to measure leaf chlorophyll concentration in Arabidopsis thaliana

2010

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“…The previously described plastid protein import mutants ppi1 (Jarvis et al, 1998) and ppi2 (Bauer et al, 2000), as well as tic40 (Chou et al, 2003) have pale, lack of chlorophyll phenotypes. These phenotypes reflect effects of the mutations on chloroplast biogenesis.…”

Section: T-dna Insertional Disruption Of Toc90mentioning

confidence: 90%

“…Ectopic expression of atToc34 rescues ppi1 indicating that atToc34 and atToc33 are functionally equivalent in vivo (Jarvis et al, 1998). There are four homologues of pea Toc159 in Arabidopsis, atToc159, -132, -120 and -90 (Hiltbrunner et al, 2001a;Jackson-Constan and Keegstra, 2001).…”

Section: Introductionmentioning

confidence: 97%

“…Strikingly the Arabidopsis homologues of the Toc34 and Toc159 GTP-binding proteins are encoded by a small gene family (Jackson-Constan and Hiltbrunner et al, 2001a). AtToc33 and atToc34, the two homologues of pea Toc34, consist of a soluble GTP-binding domain (G-domain), containing GTP-binding motifs, followed by a C-terminal hydrophobic transmembrane helix anchoring the proteins in the outer membrane, while the G-domain faces the cytosol (Jarvis et al, 1998). AtToc159, atToc132 and atToc120, highly homologous to pea Toc159, have a tripartite structure (Bauer et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

“…Disruption of atToc33 in the ppi1 mutant (plastid protein import mutant 1) results in a chlorophyll-deficient seedling phenotype due to retarded chloroplast biogenesis, but mature plants are indistinguishable from the wild type (Jarvis et al, 1998). Ectopic expression of atToc34 rescues ppi1 indicating that atToc34 and atToc33 are functionally equivalent in vivo (Jarvis et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

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AtToc90, a New GTP-Binding Component of the Arabidopsis Chloroplast Protein Import Machinery

et al. 2004

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AtToc159 is a GTP-binding chloroplast protein import receptor. In vivo, atToc159 is required for massive accumulation of photosynthetic proteins during chloroplast biogenesis. Yet, in mutants lacking atToc159 photosynthetic proteins still accumulate, but at strongly reduced levels whereas non-photosynthetic proteins are imported normally: This suggests a role for the homologues of atToc159 (atToc132, -120 and -90). Here, we show that atToc90 supports accumulation of photosynthetic proteins in plastids, but is not required for import of several constitutive proteins. Part of atToc90 associates with the chloroplast surface in vivo and with the Toc-complex core components (atToc75 and atToc33) in vitro suggesting a function in chloroplast protein import similar to that of atToc159. As both proteins specifically contribute to the accumulation of photosynthetic proteins in chloroplasts they may be components of the same import pathway.

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Nuclear‐encoded Protein Import into Chloroplasts: Methods

Soll

Bölter

2010

Encyclopedia of Life Sciences

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Chloroplasts carry out essential processes, for example photosynthesis. They are derived from an endosymbiotic event, in which an ancient cyanobacterium was engulfed by an eukaryotic ancestor. During evolution, most of the genes have been transferred to the nucleus. Consequently, >98% of all plastid proteins are translated on cytosolic ribosomes and posttranslationally targeted to and imported into the organelle. Targeting is assisted by cytosolic proteins, which keep them in an import‐competent state. At the chloroplast, many proteins have to conquer the barrier of the chloroplast envelopes. This process is mediated by two complexes in the outer (Toc) and inner (Tic) envelope. Most proteins destined for inner compartments contain a cleavable N ‐terminal transit peptide, whereas most outer envelope components insert into the membrane without such a targeting peptide. Investigation of the import of nuclear‐encoded proteins into chloroplasts is an essential field of plant science. To throw light on this very basic process many different methods have been established. Key Concepts: Studying the in vitro import behaviour of chloroplastic preproteins gives essential insight into this fundamental process. Analysis of mutants in model organisms provides information about the in vivo function of proteins proposed to be involved into translocation.

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An Arabidopsis Mutant Defective in the Plastid General Protein Import Apparatus

Cited by 317 publications

References 24 publications

Use of a SPAD-502 meter to measure leaf chlorophyll concentration in Arabidopsis thaliana

Use of a SPAD-502 meter to measure leaf chlorophyll concentration in Arabidopsis thaliana

AtToc90, a New GTP-Binding Component of the Arabidopsis Chloroplast Protein Import Machinery

Nuclear‐encoded Protein Import into Chloroplasts: Methods

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