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Cloning and Sequence Analysis of a Wheat RING Domain Ubiquitin Protein Ligase Gene

Author

Listed:
  • Zaijun Yang
  • Zhengsong Peng
  • Kai Wu
  • Shuhong Wei
  • Yonghong Zhou

Abstract

Full length cDNA sequence of RING domain ubiquitin protein ligase gene TaZFP-1 was acquired by RT-PCR methods. Then, analysis and prediction on the acquired sequences and its amino acids, physicochemical properties, hydrophobicity/hydrophilicity, secondary structure, functional domains, sequence alignment and phylogenetic tree. The results showed that TaZFP-1 gene cDNA was 759 bp in length, encoding 252 amino acids. Â Most amino acids in TaZFP-1 protein are hydrophilic amino acids, so the protein may be a soluble protein. Secondary structure of TaZFP-1 was mainly composed of a-helices and random coils. Functional domains analysis indicated that the TaZFP-1 is a RING finger domain protein and containing a C3HC4 motif. The molecular evolution threes showed that the TaZFP-1 was clustered into the monocotyledon group and high genetic relationship with O. sativa RING domain E3 ligases.

Suggested Citation

  • Zaijun Yang & Zhengsong Peng & Kai Wu & Shuhong Wei & Yonghong Zhou, 2011. "Cloning and Sequence Analysis of a Wheat RING Domain Ubiquitin Protein Ligase Gene," Modern Applied Science, Canadian Center of Science and Education, vol. 5(3), pages 164-164, June.
    • Handle: RePEc:ibn:masjnl:v:5:y:2011:i:3:p:164
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    JEL classification:

    • R00 - Urban, Rural, Regional, Real Estate, and Transportation Economics - - General - - - General
    • Z0 - Other Special Topics - - General

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