Expression, Purification And Characterization Of Lysine Methyltransferase Smyd5

Publication Year:
2017
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Abstract Views 19
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Repository URL:
https://digitalcommons.wayne.edu/oa_theses/596
Author(s):
Xue, Wen
Tags:
Biochemistry; Molecular Biology
thesis / dissertation description
Methylation of histones and non-histone proteins play vital roles in numerous cellular processes including gene expression regulation and DNA damage response. The identifications of methyltransferase SMYD protein family are not well characterized. SMYD5 is a unique and critical member of SMYD family involved in immune response, stem cell renew, hematopoiesis regulation and cancer metastasis. Understanding its function and structure is monumental to human disease. With the achievement of SMYD5 expression and purification, the association between SMYD5 and its substrate histone H4 has been investigated. While possessing a poly-E tail instead of the TPR domain included in other members, SMYD5 is assumed that associated with Calcium and could potentially be a mitochondrial protein.