The NH2‐terminal residues of rat liver proteasome (multicatalytic proteinase complex) subunits, C2, C3 and C8, are Nα‐acetylated

FEBS Letters

Aruga, Rie¹  Tanaka, Keiji¹  Tokunaga, Fuminori¹  Iwanaga, Sadaaki¹  Shimonishi, Yasutsugu¹  Takao, Toshifumi¹  Ichihara, Akira¹ 

[1] Department of Molecular Biology, Graduate School of Medical Science, Fukuoka 812, Japan

关键词: Nα-acetylation;    Proteasome;    Multicatalytic proteinase;    FAB;    fast atom bombrdment;    HPLC;    high performance liquid chromatography;   

DOI  :  10.1016/0014-5793(90)81417-M

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown