A 45 amino acid residue domain necessary and sufficient for proteolytic cleavage of the MAP1B polyprotein precursor

FEBS Letters

Tögel, Martin¹  Propst, Friedrich¹  Eichinger, René¹  Wiche, Gerhard¹ 

[1] Institute of Biochemistry and Molecular Cell Biology, Vienna Biocenter, University of Vienna, Dr. Bohr-Gasse 9, A-1030 Vienna, Austria

关键词: Microtubule-associated protein 1B;    Polyprotein precursor;    Proteolytic cleavage;    Domain structure;    Enhanced green fluorescent protein/β-galactosidase fusion protein;    MAP1B and MAP1A;    microtubule-associated proteins 1B and 1A;    GFP;    enhanced green fluorescent protein;    β-Gal;    β-galactosidase;   

DOI  :  10.1016/S0014-5793(99)00523-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The microtubule-associated proteins 1B and 1A are synthesized as polyprotein precursors which are rapidly cleaved to give rise to heavy and light chains constituting the respective microtubule-associated protein 1B or microtubule-associated protein 1A complex. To identify domains necessary for precursor processing, we expressed microtubule-associated protein 1B deletion mutants in fibroblasts and monitored proteolytic cleavage of the precursor proteins by immunoblot analysis. We found that a novel hydrophilic, proline-rich 45 amino acid domain containing the cleavage site is necessary and sufficient for processing. This domain is conserved in microtubule-associated protein 1A. Additional sequences in the N-terminal half of the heavy chain contribute to the efficiency of cleavage.

【 授权许可】

Unknown