Structural and functional characterization of yeast histone deacetylase Hos3.
Published: 2005
Language: eng
Number of pages: 105
Description: Several key residues were identified as being catalytically important in Hos3 since they inactivated the enzyme when they were mutated to alanine but left it structurally intact as revealed by circular dichroism and gel filtration chromatography. From sequence alignment these residues correspond to key catalytic residues in HDLP. Combined with the fact that both Hos3 and HDLP require a zinc ion, these results strongly suggest that Hos3 has a similar catalytic mechanism to that proposed for HDLP. With the use of chemical labeling and mass-spectrometry, Cys 197 and Cys 456 were identified as having free sulfhydryl groups. By mutating Cys 197 to alanine, aggregation of Hos3 was substantially reduced. In addition, a systematic deletion analysis revealed that Hos3p can be trimmed by more than 150 residues from its C-terminus, and is still active. However, systematic N-terminal truncations revealed that Hos3 cannot tolerate deletions of more than 30 residues.
Notes: Thesis (M.Sc.)--University of Toronto, 2005.

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Source: Masters Abstracts International, Volume: 44-01, page: 0352.

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