THE NH2-TERMINAL RESIDUES OF RAT-LIVER PROTEASOME (MULTICATALYTIC PROTEINASE COMPLEX) SUBUNITS, C2, C3 AND C8, ARE N-ALPHA-ACETYLATED

被引：26

作者：

TOKUNAGA, F

ARUGA, R

IWANAGA, S

TANAKA, K

ICHIHARA, A

TAKAO, T

SHIMONISHI, Y

机构：

[1] KYUSHU UNIV 33,GRAD SCH MED SCI,DEPT MOLEC BIOL,FUKUOKA 812,JAPAN

[2] KYUSHU UNIV 33,FAC SCI,DEPT BIOL,FUKUOKA 812,JAPAN

[3] UNIV TOKUSHIMA,INST ENZYME RES,TOKUSHIMA 770,JAPAN

[4] OSAKA UNIV,INST PROT RES,SUITA,OSAKA 565,JAPAN

来源：

FEBS LETTERS | 1990年 / 263卷 / 02期

关键词：

Multicatalytic proteinase; Nα-acetylation; Proteasome;

D O I：

10.1016/0014-5793(90)81417-M

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Rat liver proteasome (multicatalytic proteinase complex) is a 20S-ring shaped particle having a molecular mass of 750 kDa, and iscomposed of at least 13 non-identical components ranging from 21 to 31 kDa in size. We found here that the NH2-terminal residues of all the known 13 components, except for C5, are not reactive to phenylisothiocyanate. Among them, components C2, C3 and C8 are blocked in their NH2-termini with Nα-acetyl-Met, Nα-acetyl-Ala, and Nα-acetyl-Ser, respectively. The NH2-terminal portions of C2, C3, and C8 exhibit sequence similarity to one another, but that of the non-blocked component C5 differs from those of C2, C3, and C8. © 1990.

引用

页码：373 / 375

页数：3

共 9 条

[1] IDENTITY OF THE 19S PROSOME PARTICLE WITH THE LARGE MULTIFUNCTIONAL PROTEASE COMPLEX OF MAMMALIAN-CELLS (THE PROTEASOME) [J].