Purification of Chlamydomonas 28-kDa ubiquitinated protein and its identification as ubiquitinated histone H2B.
One of the most predominantly ubiquitinated protein species in Chlamydomonas, of which the apparent molecular mass in SDS-PAGE was 28 kDa, was found to exist abundantly in nuclei. The 28-kDa ubiquitinated protein was purified to homogeneity from the isolated nuclei of Chlamydomonas, and its partial amino acid sequence was determined. The N-terminal peptide sequence was identical with that of ubiquitin. Sequences homologous to those Chlamydomonas ubiquitin [corrected] and wheat histone H2B, and paired sequences of both of them were found in arginylendopeptidase-digested or protease V8-digested polypeptide fragments of the 28-kDa ubiquitinated protein. Based on these results, it was concluded that Chlamydomonas 28-kDa ubiquitinated protein is monoubiquitinated histone H2B.
Shimogawara
K
K
Institute of Applied Microbiology, University of Tokyo, Japan.
Muto
S
S
D000595:Amino Acid Sequence; D000818:Animals; D002467:Cell Nucleus / Q000737:chemistry; D016825:Chlamydomonas reinhardtii / Q000737:chemistry*; D002843:Chromatin / Q000737:chemistry; D002851:Chromatography, High Pressure Liquid; D006657:Histones / Q000737:chemistry / Q000302:isolation & purification*; D015151:Immunoblotting; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry; D014452:Ubiquitins / Q000737:chemistry / Q000302:isolation & purification*
D002843:Chromatin; D006657:Histones; D010446:Peptide Fragments; D014452:Ubiquitins