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Citation:

Characterization of a Novel Ubiquitin-conjugating Enzyme from Camellia oleifera

  • Received Date: 2012-09-26
  • Ubiquitin-conjugating enzyme (E2) is one of three key enzymes in the ubiquitin-proteasome pathway (UPP). And it's very important in the protein degradation pathways depend on ubiquitin or N-end rule, including identify the target protein, interaction with ubiquitin-protein ligating enzymes (E3), and so on. A full length cDNA sequence of E2 was cloned by Solexa sequencing technology and named UBE2-J2. This cDNA codes 239 amino acids, and has significant amino acid sequence identity and similarity with E2s from other organism. The UBE2-J2 protein has an ubiquitin-conjugating enzyme E2 catalytic (UBCc) domain from 8th to 122nd amino acid residue. There are 17 residues to compose Ubiquitin thioester intermediate interaction residues, 5 residues to compose E3 interaction residues and the 87th residue is the active site cysteine on conserved domain UBCc. UBE2-J2 is a class Ⅱ member of E2 family of Camellia oleifera according to bioinformatics analysis.
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Characterization of a Novel Ubiquitin-conjugating Enzyme from Camellia oleifera

  • 1. Research Institute of Subtropical Forestry, Chinese Academy of Forestry, Fuyang 311400, Zhejiang, China
  • 2. Dongfanghong Forest Farm of Jinhua City, Zhejiang Province, Jinhua 321025, Zhejiang, China

Abstract: Ubiquitin-conjugating enzyme (E2) is one of three key enzymes in the ubiquitin-proteasome pathway (UPP). And it's very important in the protein degradation pathways depend on ubiquitin or N-end rule, including identify the target protein, interaction with ubiquitin-protein ligating enzymes (E3), and so on. A full length cDNA sequence of E2 was cloned by Solexa sequencing technology and named UBE2-J2. This cDNA codes 239 amino acids, and has significant amino acid sequence identity and similarity with E2s from other organism. The UBE2-J2 protein has an ubiquitin-conjugating enzyme E2 catalytic (UBCc) domain from 8th to 122nd amino acid residue. There are 17 residues to compose Ubiquitin thioester intermediate interaction residues, 5 residues to compose E3 interaction residues and the 87th residue is the active site cysteine on conserved domain UBCc. UBE2-J2 is a class Ⅱ member of E2 family of Camellia oleifera according to bioinformatics analysis.

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