Peptide sequencing identifies MSS1, a modulator of HIV Tat‐mediated transactivation, as subunit 7 of the 26 S protease

FEBS Letters

Dubiel, Wolfgang²  Ferrell, Katherine¹  Rechsteiner, Martin¹ 

[1] Department of Biochemistry, University of Utah, School of Medicine, Salt Lake City, UT 84132, USA;Institut für Biochemie, Medizinische Fakultät (Charité), Humboldt-Universität zu Berlin, Hessiche Str. 3-4, O-1040 Berlin, Germany

关键词: MSS1;    HIV;    Human 26 S protease: Putative ATPase;    Tat;    SDS;    sodium dodecyl sulfate;    PAGE;    polyacrylamide gel electrophoresis;    HIV;    human immunodeficiency virus;    sLLVY-MCA;    succinyl-Leu-Leu-Val-Tyr-7-amido-4-methyl coumarin;    CNBr;    cyanogen bromide;    PVDF;    polyvinylidene difluoride;   

DOI  :  10.1016/0014-5793(93)81356-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown