PEPTIDE SEQUENCING IDENTIFIES MSS1, A MODULATOR OF HIV TAT-MEDIATED TRANSACTIVATION, AS SUBUNIT-7 OF THE 26-S PROTEASE

被引：86

作者：

DUBIEL, W ^{[1
]}

FERRELL, K ^{[1
]}

RECHSTEINER, M ^{[1
]}

机构：

[1] UNIV UTAH,SCH MED,DEPT BIOCHEM,SALT LAKE CITY,UT 84112

来源：

FEBS LETTERS | 1993年 / 323卷 / 03期

关键词：

MSS1; HIV; HUMAN-26; S-PROTEASE; PUTATIVE ATPASE; TAT;

D O I：

10.1016/0014-5793(93)81356-5

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：

Subunit 7 is an integral component of the human erythrocyte 26 S protease. Peptide sequence analysis reveals that 22 amino acids from the N-terminus of subunit 7 correspond exactly to the N-terminus of MSS1, a modulator of HIV gene expression. Additional internal peptides from subunit 7 obtained by CNBr cleavage also match 100% with the deduced amino acid sequence of MSS1. Based on the fact that directly sequenced peptides from subunit 7 are identical to more than 12% of the hypothetical translation product of MSS1, and the fact that the molecular weight of subunit 7 (49 kDa) corresponds to the predicted molecular weight of MSS1 (48,633 Da), we conclude that subunit 7 is MSS1.

引用

页码：276 / 278

页数：3

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