PROTEIN METHYLATION
PROTEIN METHYLATION
复制标题
DOI:
10.1126/science.174.4005.114
复制
发表时间:
1971-01-01
期刊:
影响因子:
56.9
通讯作者:
KIM, S
中科院分区:
文献类型:
--
作者:
PAIK, WK;KIM, S
The structure of a protein molecule is primarily determined by the se-quence of the constituent amino acids. However, the structures of certain proteins are further modified after genetic translation by alterations in the constit-uent amino acid residues. Such alterations come about as a result of, for example, hydroxylation, phosphoryla-tion, acetylation, methylation, or thio-lation. Hydroxylation of preformed protein occurs almost exclusively in collagen, and reviews have adequately dealt with this subject (1). Apart from its role in carbohydrate meta-bolism (2), phosphorylation as well as acetylation and methylation of proteins is very much studied at present partly because of the observation by Huang and Bonner that histone inhibits the DNA-dependent RNA polymerase (3), and that some specificity of histone as a gene regulator may be due to the fact that its side chains are often modified by acetyl or methyl groups (4). The phosphorylation and acetylation of histone have been reviewed (S, 6). During the last several years, studies on methylation of proteins have yielded many important observations. While these studies were going on, it was generally realizedthat protein methyla-tion is far more complex and has more ramifications than was originally as-sumed. Various amino acids are methylated, their methylation involves specific enzymes, and the occurrence of methylated amino acids in nature is extremely diverse. Thus the protein methylation process might have far-reaching effects on the control of protein function in vivo. In this article we review the present status of knowledge