衣藻28 kDa泛素化蛋白的纯化及其作为泛素化组蛋白H2B的鉴定。

Purification of Chlamydomonas 28-kDa ubiquitinated protein and its identification as ubiquitinated histone H2B.

作者信息

Shimogawara K, Muto S

机构信息

Institute of Applied Microbiology, University of Tokyo, Japan.

出版信息

Arch Biochem Biophys. 1992 Apr;294(1):193-9. doi: 10.1016/0003-9861(92)90157-r.

DOI:10.1016/0003-9861(92)90157-r

PMID:1312804

Abstract

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.

摘要

衣藻中最主要的泛素化蛋白种类之一，其在SDS-PAGE中的表观分子量为28 kDa，被发现大量存在于细胞核中。从衣藻分离的细胞核中纯化出了均一的28 kDa泛素化蛋白，并测定了其部分氨基酸序列。N端肽序列与泛素的相同。在28 kDa泛素化蛋白的精氨酰内肽酶消化或蛋白酶V8消化的多肽片段中发现了与衣藻泛素[校正后]和小麦组蛋白H2B同源的序列，以及它们两者的配对序列。基于这些结果，得出结论：衣藻28 kDa泛素化蛋白是单泛素化的组蛋白H2B。