Localization of the pro-sequence within the total deduced primary structure of human beta-hexosaminidase B.
Article Details
- CitationCopy to clipboard
Stirling J, Leung A, Gravel RA, Mahuran D
Localization of the pro-sequence within the total deduced primary structure of human beta-hexosaminidase B.
FEBS Lett. 1988 Apr 11;231(1):47-50.
- PubMed ID
- 2966076 [ View in PubMed]
- Abstract
The beta subunit of beta-hexosaminidase (beta-N-acetylhexosaminidase, EC 3.2.1.52) is synthesized in the rough endoplasmic reticulum as a prepropolypeptide. After the loss of the signal peptide and formation of an enzymatically active dimer, the pro-enzyme is either secreted from the cell or transported into the lysosome for processing to its mature form. In order to characterize the early posttranslational events we have purified nearly 1 mg of pro-hexosaminidase B from the NH4Cl containing medium of fibroblasts derived from a patient with the infantile form of Tay-Sachs disease. The partial N-terminal sequence was mapped to a position 42 residues C-terminal to the first in-frame ATG (Met residue) and 79 residues N-terminal to the known mature N-terminus. This position corresponds to that predicted for the cleavage of a 17 amino acid signal peptide generated through the use of the third rather than the first in-frame ATG as the initiation site for protein synthesis.