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Analysis of Lysine‐Rich Histones From the Unicellular Green Alga Chlamydomonas Reinhardtii
Author(s) -
MORRIS RODNEY L.,
SALINGER ANDREW P.,
RIZZO PETER J.
Publication year - 1999
Publication title -
journal of eukaryotic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 1066-5234
DOI - 10.1111/j.1550-7408.1999.tb05142.x
Subject(s) - chlamydomonas reinhardtii , biology , chlamydomonas , lysine , histone , green algae , botany , algae , microbiology and biotechnology , genetics , gene , amino acid , mutant
The H1 histones of the unicellular green alga Chlamydomonas reinhardtii were extracted from isolated nuclei, fractionated by high performance liquid chromatography, and analyzed by two‐dimensional electrophoresis. peptide mapping, and N‐terminal sequencing. Sodium dodecyl sulfate polyacrylamide gel electrophoresis of 5% perchloric acid extracts of isolated C. reinhardtii nuclei revealed two H1 proteins (H1A and H1B). Two‐dimensional gel analysis did not reveal heterogeneity of either algal H1 protein, but did detect differences in the hydrophobic amino acid content of the C. reinhardtii H1A and H1B. Digestion of H1A and H1B with V8 protease revealed two distinctly different peptide maps. C. reinhardtii H1 peptide maps were not at all similar to those of Pisum H1, but algal and pea H2B peptide maps did show some peptides in common. Seventeen amino acid residues were obtained from C. reinhardtii H1A amino terminal sequencing, while the H1B N‐terminus was blocked. A search of protein data bases revealed no sequence homology of the H1A N‐terminus with any known protein. Chlamydomonas histones fractionated by high performance liquid chromatography revealed minor components (histone variants) for H2A and H2B. the amino acid composition of Chlamydomonas lysinerich histones was compared to those of various other unicellular algae.