Article ; Online: Cloning Strategy for HDAC1/HDAC2 Hybrid Protein Expression in Mammalian Cells.
Methods in molecular biology (Clifton, N.J.)
2022 Volume 2589, Page(s) 401–409
Abstract: Dynamic deacetylation of non-histone proteins by histone deacetylases (HDACs) is a key regulator of protein functions, interactions, and turnover. Among class I HDACs, human HDAC1 and HDAC2 share more than 80% global homology at the amino acid level. ... ...
Abstract | Dynamic deacetylation of non-histone proteins by histone deacetylases (HDACs) is a key regulator of protein functions, interactions, and turnover. Among class I HDACs, human HDAC1 and HDAC2 share more than 80% global homology at the amino acid level. However, despite the high redundancy, there are examples for differential substrate specificities of HDAC1 and HDAC2. Until now it remains quite unclear how specific and overlapping functions of HDAC1/HDAC2 are regulated in different contexts. Here, we describe molecular cloning techniques for the generation of HDAC1/HDAC2 hybrid proteins, HDAC1/HDAC2 mutants lacking known interaction domains, and HDAC1/HDAC2 hybrid proteins with interchanged N-terminal domains. These proteins are tools for the analysis of specific protein interactions and functions in mammalian cells. |
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MeSH term(s) | Animals ; Humans ; Histone Deacetylase 2/genetics ; Histone Deacetylase 2/metabolism ; Histone Deacetylase 1/genetics ; Histone Deacetylase 1/metabolism ; Histone Deacetylases/metabolism ; Amino Acids ; Cloning, Molecular ; Mammals/metabolism |
Chemical Substances | Histone Deacetylase 2 (EC 3.5.1.98) ; Histone Deacetylase 1 (EC 3.5.1.98) ; Histone Deacetylases (EC 3.5.1.98) ; Amino Acids ; HDAC1 protein, human (EC 3.5.1.98) ; HDAC2 protein, human (EC 3.5.1.98) |
Language | English |
Publishing date | 2022-10-18 |
Publishing country | United States |
Document type | Journal Article |
ISSN | 1940-6029 |
ISSN (online) | 1940-6029 |
DOI | 10.1007/978-1-0716-2788-4_26 |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
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