Replacement of the C-terminal tetrapeptide (314PAPV317 to 314SSSM317) in interferon regulatory factor-2 alters its N-terminal DNA-binding activity

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• 作者：Krishna Prakash ; Pramod C. Rath
• 关键词：Conformation ; DNA ; binding ; IRF ; 2 ; tetrapeptide
• 刊名：Journal of Biosciences
• 出版年：2010
• 出版时间：December 2010
• 年：2010
• 卷：35
• 期：4
• 页码：547-556
• 全文大小：
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• 作者单位：Krishna Prakash (1)
  Pramod C. Rath (1)
  
  1. Molecular Biology Laboratory, School of Life Sciences, Jawaharlal Nehru University, New Delhi, 110 067, India
  
• 刊物类别：Life Sciences, general; Biomedicine general; Zoology; Plant Sciences; Microbiology; Cell Biology;
• 刊物主题：Life Sciences, general; Biomedicine general; Zoology; Plant Sciences; Microbiology; Cell Biology;
• 出版者：Springer India
• ISSN：0973-7138

文摘

Interferon regulatory factor-2 (IRF-2) is an important transcription factor involved in cell growth regulation, immune response and cancer. IRF-2 can function as a transcriptional repressor and activator depending on its DNA-binding activity and protein-protein interactions. We compared the amino acid sequences of IRF-2 and found a C-terminal tetrapeptide (314PAPV317) of mouse IRF-2 to be different (314SSSM317) from human IRF-2. Recombinant GST-IRF-2 with 314PAPV317 (wild type) and 314SSSM317 (mutant) expressed in Escherichia coli were assessed for DNA-binding activity with 32P-(GAAAGT)₄ by electrophoretic mobility shift assay (EMSA). Wild type- and mutant GST-IRF-2 showed similar expression patterns and immunoreactivities but different DNA-binding activities. Mutant (mt) IRF-2 formed higher-molecular-mass, more and stronger DNA-protein complexes in comparison to wild type (wt) IRF-2. Anti-IRF-2 antibody stabilized the DNA-protein complexes formed by both wt IRF-2 and mt IRF-2, resolving the differences. This suggests that PAPV and SSSM sequences at 314鈥?17 in the C-terminal region of mouse and human IRF-2 contribute to conformation of IRF-2 and influence DNA-binding activity of the N-terminal region, indicating intramolecular interactions. Thus, evolution of IRF-2 from murine to human genome has resulted in subtle differences in C-terminal amino acid motifs, which may contribute to qualitative changes in IRF-2-dependent DNA-binding activity and gene expression. Keywords Conformation DNA-binding IRF-2 tetrapeptide