Skip to main content
NCBI home page
Plant Physiology logoLink to Plant Physiology
. 1977 Sep;60(3):422–429. doi: 10.1104/pp.60.3.422

Analysis of the Subunit Structure of Protochlorophyllide Holochrome by Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis 1

Ora D Canaani a, Kenneth Sauer a
PMCID: PMC542629  PMID: 16660106

Abstract

The subunit structures of protochlorophyllide holochrome (PCH) and chlorophyllide holochrome (CH) were studied by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis. PCH from leaves of dark-grown (Phaseolus vulgaris var. red kidney) is a polymeric pigment-protein complex of approximately 600,000 daltons. It is composed of 12 to 14 polypeptides of 45,000 daltons, when examined prior to and immediately following photoconversion. The protochlorophyllide or chlorophyllide pigment molecules are associated with these polypeptides. Subsequent to photoconversion, the absorption maximum of newly formed chlorophyllide shifts from 678 nm to 674 nm upon standing in darkness. Following the 678 to 674 spectral shift, the chlorophyllide is associated with a polypeptide with a molecular weight of 16,000 daltons. In addition, sucrose gradient centrifugation of PCH and CH under nondenaturing conditions indicates that during the course of the dark spectroscopic shift, the 600,000 dalton CH undergoes dissociation into a small chlorophyllide protein. The dissociation of CH, the change in the molecular weight of the chlorophyllide polypeptide from 45,000 to 16,000 daltons, as well as the dark spectroscopic shift are temperature-dependent and blocked below 0 C. It was also found that each holochrome molecule of 600,000 daltons contains at least four protochlorophyllide pigment molecules.

Full text

PDF
422

Selected References

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

  1. Akoyunoglou G., Argyroudi-Akoyunoglou J. H., Guiali A., Dassiou C. On the relationship between ribulose diphosphate carboxylase and protochlorophyllide holochrome of Phaseolus vulgaris leaves. Plant Physiol. 1970 Apr;45(4):443–446. doi: 10.1104/pp.45.4.443. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Alscher R. G., Hawkes S. P., Sauer K. The association of protein synthesis with protochlorophyllide holochrome regeneration in dark-grown barley leaves. Biochem Biophys Res Commun. 1976 Nov 22;73(2):240–247. doi: 10.1016/0006-291x(76)90699-9. [DOI] [PubMed] [Google Scholar]
  3. BOARDMAN N. K. Studies on a protochlorophyll-protein complex. I. Purification and molecular-weight determination. Biochim Biophys Acta. 1962 Jul 30;62:63–79. doi: 10.1016/0006-3002(62)90492-4. [DOI] [PubMed] [Google Scholar]
  4. Butler W. L., Briggs W. R. The relation between structure and pigments during the first stages of proplastid greening. Biochim Biophys Acta. 1966 Jan 4;112(1):45–53. doi: 10.1016/s0926-6585(96)90006-0. [DOI] [PubMed] [Google Scholar]
  5. Henningsen K. W., Thorne S. W., Boardman N. K. Properties of Protochlorophyllide and Chlorophyll(ide) Holochromes from Etiolated and Greening Leaves. Plant Physiol. 1974 Mar;53(3):419–425. doi: 10.1104/pp.53.3.419. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Kahn A., Boardman N. K., Thorne S. W. Energy transfer between protochlorophyllide molecules: evidence for multiple chromophores in the photoactive protochlorophyllide-protein complex vivo and in vitro. J Mol Biol. 1970 Feb 28;48(1):85–101. doi: 10.1016/0022-2836(70)90220-2. [DOI] [PubMed] [Google Scholar]
  7. 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]
  8. Mathis P., Sauer K. Circular dichroism studies on the structure and the photochemistry of protochlorophyllide and chlorophyllide holochrome. Biochim Biophys Acta. 1972 Jun 23;267(3):498–511. doi: 10.1016/0005-2728(72)90178-8. [DOI] [PubMed] [Google Scholar]
  9. Schopfer P., Siegelman H. W. Purification of protochlorophyllide holochrome. Plant Physiol. 1968 Jun;43(6):990–996. doi: 10.1104/pp.43.6.990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Schultz A., Sauer K. Circular dichroism and fluorescence changes accompanying the protochylorophyllide to chlorophyllide transformation in greening leaves and holochrome preparations. Biochim Biophys Acta. 1972 May 25;267(2):320–340. doi: 10.1016/0005-2728(72)90120-x. [DOI] [PubMed] [Google Scholar]
  11. Strotmann H., Hesse H., Edelmann K. Quantitative determination of coupling factor CF1 of chloroplasts. Biochim Biophys Acta. 1973 Aug 31;314(2):202–210. doi: 10.1016/0005-2728(73)90135-7. [DOI] [PubMed] [Google Scholar]
  12. Thorne S. W. The greening of etiolated bean leaves. I. The initial photoconversion process. Biochim Biophys Acta. 1971 Jan 12;226(1):113–127. doi: 10.1016/0005-2728(71)90183-6. [DOI] [PubMed] [Google Scholar]

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

RESOURCES