Skip to main content
PMC home page
Plant Physiology logoLink to Plant Physiology
. 1987 Dec;85(4):971–977. doi: 10.1104/pp.85.4.971

Regulation of Light-Harvesting Chlorophyll Protein Biosynthesis in Greening Seedlings 1

A Species Comparison

James N Mathis 1,2,3,2, Kent O Burkey 1,2,3
PMCID: PMC1054378  PMID: 16665840

Abstract

The biosynthesis of the chlorophyll a/b binding protein associated with photosystem II (LHC-II) was characterized during light-induced greening of etiolated barley (Hordeum vulgare [L.] cv Boone), maize (Zea mays [L.] Pioneer 3148), pea (Pisum sativum [L.] cv Progress 9), and soybean (Glycine max [L.] Merr. cv Ransom 2). Northern blot analysis revealed that pea LHC-II mRNA was present in dark-grown seedlings and accumulated rapidly within 1 hour following illumination with white light. In contrast, the accumulation of LHC-II mRNA was delayed in barley and soybean until 2 to 4 hours after illumination began. Single radial immunodiffusion analysis revealed that LHC-II polypeptides began to accumulate in all species between 4 and 8 hours although the protein was present in detectable levels at earlier times in certain species. In a pattern similar to the LHC-II protein accumulation, chlorophyll accumulated at increased rates between 4 and 8 hours of greening in all species following an initial delay. The absence of coordination between LHC-II mRNA and LHC-II protein accumulation that was clearly observed in pea suggested that transcription is not the factor that limits LHC-II complex formation during chloroplast development. The accumulation of chlorophyll and LHC-II protein appeared to coincide suggesting that chlorophyll biosynthesis may be a factor that limits LHC-II complex formation.

Full text

PDF
971

Images in this article

973Fig. 1
on p.973
973Fig. 2
on p.973
974Fig. 3
on p.974
975Fig. 4
on p.975

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Camm E. L., Green B. R. Fractionation of Thylakoid Membranes with the Nonionic Detergent Octyl-beta-d-glucopyranoside: RESOLUTION OF CHLOROPHYLL-PROTEIN COMPLEX II INTO TWO CHLOROPHYLL-PROTEIN COMPLEXES. Plant Physiol. 1980 Sep;66(3):428–432. doi: 10.1104/pp.66.3.428. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Cashmore A. R. Structure and expression of a pea nuclear gene encoding a chlorophyll a/b-binding polypeptide. Proc Natl Acad Sci U S A. 1984 May;81(10):2960–2964. doi: 10.1073/pnas.81.10.2960. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Cline K., Werner-Washburne M., Lubben T. H., Keegstra K. Precursors to two nuclear-encoded chloroplast proteins bind to the outer envelope membrane before being imported into chloroplasts. J Biol Chem. 1985 Mar 25;260(6):3691–3696. [PubMed] [Google Scholar]
  4. Coruzzi G., Broglie R., Cashmore A., Chua N. H. Nucleotide sequences of two pea cDNA clones encoding the small subunit of ribulose 1,5-bisphosphate carboxylase and the major chlorophyll a/b-binding thylakoid polypeptide. J Biol Chem. 1983 Feb 10;258(3):1399–1402. [PubMed] [Google Scholar]
  5. Cuming A. C., Bennett J. Biosynthesis of the light-harvesting chlorophyll a/b protein. Control of messenger RNA activity by light. Eur J Biochem. 1981 Aug;118(1):71–80. doi: 10.1111/j.1432-1033.1981.tb05487.x. [DOI] [PubMed] [Google Scholar]
  6. Dunsmuir P., Smith S. M., Bedbrook J. The major chlorophyll a/b binding protein of petunia is composed of several polypeptides encoded by a number of distinct nuclear genes. J Mol Appl Genet. 1983;2(3):285–300. [PubMed] [Google Scholar]
  7. Gollmer I., Apel K. The phytochrome-controlled accumulation of mRNA sequences encoding the light-harvesting chlorophyll a/b protein of barley (Hordeum vulgare L.). Eur J Biochem. 1983 Jun 15;133(2):309–313. doi: 10.1111/j.1432-1033.1983.tb07463.x. [DOI] [PubMed] [Google Scholar]
  8. Grossman A. R., Bartlett S. G., Schmidt G. W., Mullet J. E., Chua N. H. Optimal conditions for post-translational uptake of proteins by isolated chloroplasts. In vitro synthesis and transport of plastocyanin, ferredoxin-NADP+ oxidoreductase, and fructose-1,6-bisphosphatase. J Biol Chem. 1982 Feb 10;257(3):1558–1563. [PubMed] [Google Scholar]
  9. Karlin-Neumann G. A., Kohorn B. D., Thornber J. P., Tobin E. M. A chlorophyll a/b-protein encoded by a gene containing an intron with characteristics of a transposable element. J Mol Appl Genet. 1985;3(1):45–61. [PubMed] [Google Scholar]
  10. Kaufman L. S., Thompson W. F., Briggs W. R. Different Red Light Requirements for Phytochrome-Induced Accumulation of cab RNA and rbcS RNA. Science. 1984 Dec 21;226(4681):1447–1449. doi: 10.1126/science.226.4681.1447. [DOI] [PubMed] [Google Scholar]
  11. Kirchanski S. J., Park R. B. Comparative Studies of the Thylakoid Proteins of Mesophyll and Bundle Sheath Plastids of Zea mays. Plant Physiol. 1976 Sep;58(3):345–349. doi: 10.1104/pp.58.3.345. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Krupa Z., Huner N. P., Williams J. P., Maissan E., James D. R. Development at Cold-Hardening Temperatures : The Structure and Composition of Purified Rye Light Harvesting Complex II. Plant Physiol. 1987 May;84(1):19–24. doi: 10.1104/pp.84.1.19. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  14. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  15. Lehrach H., Diamond D., Wozney J. M., Boedtker H. RNA molecular weight determinations by gel electrophoresis under denaturing conditions, a critical reexamination. Biochemistry. 1977 Oct 18;16(21):4743–4751. doi: 10.1021/bi00640a033. [DOI] [PubMed] [Google Scholar]
  16. Martineau B., Taylor W. C. Photosynthetic gene expression and cellular differentiation in developing maize leaves. Plant Physiol. 1985 Jun;78(2):399–404. doi: 10.1104/pp.78.2.399. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Miller R. A., Zalik S. Effect of Light Quality, Light Intensity and Temperature on Pigment Accumulation in Barley Seedlings. Plant Physiol. 1965 May;40(3):569–574. doi: 10.1104/pp.40.3.569. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Moran R. Formulae for determination of chlorophyllous pigments extracted with n,n-dimethylformamide. Plant Physiol. 1982 Jun;69(6):1376–1381. doi: 10.1104/pp.69.6.1376. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Norgard M. V. Rapid and simple removal of contaminating RNA from plasmid DNA without the use of RNase. Anal Biochem. 1981 May 1;113(1):34–42. doi: 10.1016/0003-2697(81)90040-3. [DOI] [PubMed] [Google Scholar]
  20. Pichersky E., Bernatzky R., Tanksley S. D., Breidenbach R. B., Kausch A. P., Cashmore A. R. Molecular characterization and genetic mapping of two clusters of genes encoding chlorophyll a/b-binding proteins in Lycopersicon esculentum (tomato). Gene. 1985;40(2-3):247–258. doi: 10.1016/0378-1119(85)90047-2. [DOI] [PubMed] [Google Scholar]
  21. Yang R., Lis J., Wu R. Elution of DNA from agarose gels after electrophoresis. Methods Enzymol. 1979;68:176–182. doi: 10.1016/0076-6879(79)68012-6. [DOI] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES