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A 45 amino acid residue domain necessary and sufficient for proteolytic cleavage of the MAP1B polyprotein precursor
Author(s) -
Tögel Martin,
Eichinger René,
Wiche Gerhard,
Propst Friedrich
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00523-2
Subject(s) - cleavage (geology) , microtubule , amino acid , biochemistry , chemistry , residue (chemistry) , tubulin , mutant , proteolysis , microbiology and biotechnology , biology , enzyme , gene , paleontology , fracture (geology)
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.