Polypeptide composition of thylakoids from viridis and xantha mutants in barley

Machold, O.; Høyer‐Hansen, Gunilla

doi:10.1007/bf02906144

Cited by 24 publications

(13 citation statements)

References 14 publications

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“…Several PSIIdeficient barley mutants which lack the 46,000 dalton lamellar polypeptide have now been identified; in many cases the loss of the 46,000 dalton polypeptide is accompanied by the reduction or loss of a polypeptide migrating in the 32,000 dalton region of the gel (24,36,37). In barley these lesions are accompanied by the loss of the major subunits of the chloroplast coupling factor and several other unidentified polypeptides.…”

Section: Resultsmentioning

confidence: 99%

Characterization of Three Photosystem II Mutants in Zea mays L. Lacking a 32,000 Dalton Lamellar Polypeptide

Leto¹,

Miles²

1980

Plant Physiol.

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Two fully blocked and one partially blocked photosystem II nuclear mutants have been selected in Zea mays. The fully blocked mutants lack photosystem II activity, variable fluorescence, the light-inducible C-550 signal, the high potential form of cytochrome b-559, and most or all of the low potential form of the cytochrome. The block in these mutants may primarily affect the reducing side of photosystem II, inasmuch as chloroplasts isolated from both mutants exhibit an elevated F695 fluorescence emission peak. The partially blocked mutant exhibits partial photosystem 11 activity and a reduction, but not the total loss of the variable fluorescence yield, the C-550 signal, and the high potential form of cytochrome b-559. Lamellae isolated from the fully blocked mutants are greatly deficient for a major lamellar polypeptide with an apparent molecular weight of 32,000 daltons, whereas lamellae from the partially blocked mutant show the partial loss of this same polypeptide, suggesting that the 32,000 dalton polypeptide is necessary for the proper function of photosystem I.Genetic mutants are useful tools for the study of photosynthesis, as has been amply documented in the classic work with algal photosynthetic mutants (22). However, with the exception of the large collection of well characterized pigment mutants in barley (17, 36), the number of photosynthesis mutants studied in any single species of flowering plant has been relatively small. To date, most higher plant photosynthesis mutants are characterized by gross pigment losses which are often accompanied by major alterations in thylakoid membrane morphology and the loss of many lamellar polypeptides (9,15,36,37). Recently, a large collection of photosynthesis mutants was obtained in Zea mays (28) using elevated levels of Chl fluorescence to screen specifically for mutants blocked in photosynthesis (29). By employing this technique, both fully green and yellow-green nuclear mutants with blocks in electron transport, photophosphorylation, and dark reactions have been identified (26,28).The present study describes the characteristics of three nuclear photosynthesis mutants in maize. Two of these mutants, hcf*-33 and hcf*-19G, are fully blocked in PSII, whereas a third mutant, hcf*-19YG, is partially blocked in PSII. All three mutations affect not only PSII activity, but also cause the loss of one or both redox

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Section: Resultsmentioning

confidence: 99%

Characterization of Three Photosystem II Mutants in Zea mays L. Lacking a 32,000 Dalton Lamellar Polypeptide

Leto¹,

Miles²

1980

Plant Physiol.

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“…Recently, the five different subunits of coupling factor (CF1) were identified in the SDS-PAGE electrophoretogram of total barley polypeptides by the use of antibodies raised against purified CFt and crossed immunoelectrophoresis (22). A different approach is based on comparison of the electrophoretogram of wild-type thylakoid polypeptides with those of mutants with known photosynthetic lesions (28). Photosynthetic mutants available from higher plants have generally been selected due to alterations in their pigment content (!…”

Section: Introductionmentioning

confidence: 99%

A photosystem I mutant in barley (Hordeum vulgare L.)

Møller

Smillie

Høyer‐Hansen

1980

Carlsberg Res. Commun.

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The nuclear gene mutant viridis-n 34 in barley has been characterized as a photosystem I mutant. The slow component of the light dependent absorption change at 518 nm and the photooxidation of cytochrome f were greatly reduced in mutant leaves compared with wild-type leaves. The oxidation of cytochrome f in mutant leaves irradiated with far-red light was only 7 % of the value obtained with wild-type. The fast component of the 518 nm absorbance change was similar in wild-type and mutant leaves. The rate of photosystem I electron transport in the mutant is approximately 10% of the rate observed with wild-type thylakoids whereas photosystem II electron transport appears normal. Little or no P700 was detected in the mutant. The levels of cytochromes and ferredoxin-NADP § oxidoreductase were normal. Mutant thylakoids were unable to generate a proton gradient upon illumination. Analysis of the polypeptide composition of thylakoids of viridis-n 34 revealed that these are depleted in chlorophyll a-protein 1 and three polypeptides believed to be iron-sulfur proteins. These four polypeptides are components of photosystem I particles isolated from wild-type barley.Abbreviations: Asc = ascorbic acid, Chl = chlorophyll, Cyt = cytochrome, DBMIB = dibromothymoquinone, DCIP = 2,6-dichlorophenolindophenol, DCMU = 3-(3,4-dichlorophenyl)--l,l-dimethylurea, DTT = dithiothreitol, FeCN = potassium ferricyanide, GD --Gramicidin D, MeV = methylviologen, NADP § = {~-nicotinamide adenine dinucleotide phosphate, PD --p-phenylenediamine, PS = photosystem, SDS-PAGE --sodium dodecyl sulfate polyacrylamide gel electrophoresis, TMPD = N,N,N',N'-tetramethylphenylenediamine, Tricine --N-(tris-(hydroxymethyl)-methyl)glycine, Tris = tris-(hydroxymethyl)aminomethane.

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“…Mutants in which one or a few membrane polypeptides are strongly reduced in amounts or missing as well as mutants containing new polypeptides are powerful tools in helping to characterize the membrane proteins and their function (e.g. I, 3,4,15,16,17). Previous work on the characterization of the lamellar proteins of barley chloroplast mutants in the Copenhagen stock collection was carried out by membrane solubilization with phenolacetic acid-urea and based on an analysis of chloroplast membrane development during greening of etioplasts in wild type barley (17).…”

Section: Introductionmentioning

confidence: 99%

Polypeptide composition of internal membranes from barley etioplasts

Høyer‐Hansen

Machold²,

Kahn

1976

Carlsberg Res. Commun.

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The polypeptides of isolated etioplast membranes and chloroplast membranes were solubilized in sodium dodecyl sulfate. Protein band patterns were obtained by electrophoresis on polyacrylamide slab gels with separating gels containing either a uniform polyacrylamide concentration or a concentration gradient. Several characteristic chloroplast bands were absent or reduced in intensity in patterns of etioplast membranes. Conversely, certain bands found in etioplast membrane patterns were reduced or absent in patterns of chloroplast membranes. Among these was a distinct doublet detected only in patterns of etioplast membrane polypeptides obtained with gels lacking urea. Some bands, for example those tentatively identified as subunits of coupling factor were found in patterns of etioplast as well as chIoroplast membranes.

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Polypeptide composition of thylakoids from viridis and xantha mutants in barley

Cited by 24 publications

References 14 publications

Characterization of Three Photosystem II Mutants in Zea mays L. Lacking a 32,000 Dalton Lamellar Polypeptide

Characterization of Three Photosystem II Mutants in Zea mays L. Lacking a 32,000 Dalton Lamellar Polypeptide

A photosystem I mutant in barley (Hordeum vulgare L.)

Polypeptide composition of internal membranes from barley etioplasts

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