Polypeptide composition of internal membranes from barley etioplasts

Høyer‐Hansen, Gunilla; Machold, O.; Kahn, Albert

doi:10.1007/bf02906143

Cited by 16 publications

(14 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Light induced some significant changes in the protein composition of the different membrane samples (Fig. 1) (see also [16] …”

Section: Light-induced Itwvtion Of the Light-harvesting Chlorophyll Amentioning

confidence: 90%

“…Light induced some significant changes in the protein composition of the different membrane samples ( Fig. 1) (see also [16] One possible site at which light could control the appearance of the light-harvesting chlorophyll aih protein is the level of transcription. Most eukaryotic mRNA contains poly(A) sequences [18] which facilitate isolation of this RNA fraction by affinity chromatography.…”

Section: Light-induced Itwvtion Of the Light-harvesting Chlorophyll Amentioning

confidence: 94%

See 1 more Smart Citation

The Plastid Membranes of Barley (Hordeum vulgare)

Apel

Kloppstech

1978

European Journal of Biochemistry

311

120

View full text Add to dashboard Cite

Illumination of dark‐grown barley plants induces a massive insertion of the light‐harvesting chlorophyll a/b protein into the developing thylakoid membrane. In addition to the onset of chlorophyll synthesis, light induces specifically the appearance of a prominent mRNA species which codes for a polypeptide of Mr 29500. This component was identified as a precursor of the apoprotein of the light‐harvesting chlorophyll a/b protein. The precursor has an Mr larger than the authentic protein by approximately 4000. Studies of the chlorophyll‐b‐less mutant chlorina f2 of barley offer the first clue to the mechanism which controls the light‐dependent mRNA formation. The induction of the mRNA coding for the apoprotein of the light‐harvesting chlorophyll a/b protein does not seem to be linked directly to the assembly process of the light‐harvesting structure and does not require chlorophyll b. It is proposed that light exerts its influence on the mRNA formation by a reaction which is different from the phototransformation of protochlorophyll(ide) to chlorophyll(ide).

show abstract

“…Light induced some significant changes in the protein composition of the different membrane samples (Fig. 1) (see also [16] …”

Section: Light-induced Itwvtion Of the Light-harvesting Chlorophyll Amentioning

confidence: 90%

Section: Light-induced Itwvtion Of the Light-harvesting Chlorophyll Amentioning

confidence: 94%

The Plastid Membranes of Barley (Hordeum vulgare)

Apel

Kloppstech

1978

European Journal of Biochemistry

311

120

View full text Add to dashboard Cite

show abstract

“…It is clear that extensive accumulation of the chlorophyll-binding form of the P700 chlorophyll a-protein roughly parallels the increase in chlorophyll content of developing chloroplasts (18)(19)(20) . Electrophoretic analyses of etioplast and chloroplast membrane polypeptides also suggest that the apoprotein is absent from etioplasts, or present at much lower levels than in mature chloroplasts (21)(22)(23) . However, the relationship between synthesis ofthe apoprotein and accumulation ofthe chlorophyll-protein has not been studied.…”

mentioning

confidence: 99%

Regulation of synthesis of the photosystem I reaction center.

Vierling¹,

Alberte²

1983

The Journal of Cell Biology

View full text Add to dashboard Cite

The in vivo biosynthesis of the P700 chlorophyll a-apoprotein was examined to determine whether this process is light regulated and to determine its relationship to chlorophyll accumulation during light-induced chloroplast development in barley (Hordeum vulgare L.). Rabbit antibodies to the 58,000-62,000-mol-wt apoprotein were used to measure relative synthesis rates by immunoprecipitation of in vivo labeled leaf proteins and to detect apoprotein accumulation on nitrocellulose protein blots. 5-d-old, dark-grown barley seedlings did not contain, or show net synthesis of, the 58,000-62,000-mol-wt polypeptide . When dark-grown barley seedlings were illuminated, net synthesis of the apoprotein was observed within the first 15 min of illumination and accumulated apoprotein was measurable after 1 h . After 4 h, P700 chlorophyll a-apoprotein biosynthesis accounted for up to 10% of the total cellular membrane protein synthesis . Changes in the rate of synthesis during chloroplast development suggest coordination between production of the 58,000-62,000-mol-wt polypeptide and the accumulation of chlorophyll . However, when plants were returned to darkness after a period of illumination (4 h) P700 chlorophyll a-apoprotein synthesis continued for a period of hours though at a reduced rate . Thus we found that neither illumination nor the rate of chlorophyll synthesis directly control the rate of apoprotein synthesis . The rapidity of the light-induced change in net synthesis of the apoprotein indicates that this response is tightly coupled to the primary events of light-induced chloroplast development . The data also demonstrate that de novo synthesis of the apoprotein is required for the onset of photosystem I activity in greening seedlings .The etioplasts present in leaves of dark-grown plants are predifferentiated organelles which contain many ofthe soluble and membrane protein components required for photosynthesis, but which are devoid of chlorophyll and organized photosynthetic membranes (1) . When dark-grown seedlings are illuminated, photosynthetic activity appears early and increases rapidly as a result of the rapid production and assembly of the thylakoid membrane components. The chlorophyll-binding proteins, the chlorophyll a/b-protein and the P700 chlorophyll a-protein, account for the majority of thylakoid membrane protein (2) . Therefore, the control of biosynthesis of these proteins is fundamental to both photosynthetic membrane development and chloroplast biogenesis.Recently a number of control points in the regulation of chlorophyll a/b-protein synthesis has been investigated in several species of higher plants (3-9) and in the green alga Chlamydomonas (10, 11). The apoprotein of this complex is composed of one or more subunits of^-28,000 mol wt which 1806

show abstract

“…41, No 6, 1976 designated as J. Mutants with a tendency for stacking of thylakoids into giant grana and deficient in stroma thylakoids were deficient in the high molecular weight chloroplast membrane protein B. In continuation of studies on the characterization of thylakoid proteins from barley mutants using membrane solubilization with sodium dodecyl sulfate (SDS) (12) and various conditions for electrophoresis (8) we report here on the thylakoid membrane pattern of four lethal nuclear gene mutants. Two of these are representative for the above mentioned two groups, mutant xantha-b '2 producing giant grana and mutant viridis-k z3 (like xantha-135) being defective in the conversion of Mg-protoporphyrin to protochlorophyllide (7).…”

Section: ! Introductionmentioning

confidence: 99%

Polypeptide composition of thylakoids from viridis and xantha mutants in barley

Machold¹,

Høyer‐Hansen

1976

Carlsberg Res. Commun.

Self Cite

View full text Add to dashboard Cite

The chloroplast membrane proteins from four recessive nuclear gene mutants of barley were studied with sodium dodecyl sulfate gel electrophoresis. The protein patterns of two mutants, xantha-b ~2 and viridis-zd6L consist of a summation of the polypeptides present in the chloroplast and etioplast membranes of the wild type. The pattern of viridis-c 12, a mutant deficient in photosystem I1 activity was lacking two bands, one of which is considered to be a component of the reaction center of photosystem 11. The pattern of viridis-k 23 lacked three chloroplast specific hands, two of which are components of chlorophyll-protein complex II. The results are discussed in relation to previously established functional and structural characteristics of the mutant plastids.

show abstract

Polypeptide composition of internal membranes from barley etioplasts

Cited by 16 publications

References 18 publications

The Plastid Membranes of Barley (Hordeum vulgare)

The Plastid Membranes of Barley (Hordeum vulgare)

Regulation of synthesis of the photosystem I reaction center.

Polypeptide composition of thylakoids from viridis and xantha mutants in barley

Contact Info

Product

Resources

About