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Cloning and expression analysis of a ubiquitin gene (Ub L40 ) in the haemocytes of Crassostrea hongkongensis under bacterial challenge

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Abstract

Ubiquitin, a highly conserved stress-related protein, is assigned multiple functions, such as DNA processing, protein degradation, and ribosome synthesis. The Crassostrea hongkongensis ubiquitin gene (designated ChUb L40 ) was cloned by a combination of suppressive subtractive hybridization (SSH) and rapid amplification of cDNA ends (RACE). The full-length cDNA of ChUb L40 is 496 bp in length, consisting of a 5′ untranslated region (UTR) of 34 bp, a 3′-UTR of 75 bp and an open reading frame of 387 bp encoding a ubiquitin fusion protein of 128 amino acids. Analysis of the amino acid sequence of ChUb L40 reveals that Ub L40 is highly conservative during evolution. The expression patterns of ChUb L40 gene in various tissues were examined by real-time PCR. The expression level of ChUb L40 in haemocytes is down-regulated at 4 h and gradually returned to its original level from 6 h to 24 h after Vibrio alginolyticus challenge. Our results suggest that ChUb L40 is ubiquitously expressed and plays an important role in immune defense against bacterial challenge.

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Correspondence to Ziniu Yu  (喻子牛).

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Supported by the National Basic Research Program of China (973 Program) (No. 2010CB126404), the CAS/SAFEA International Partnership Program for Creative Research Teams (No. KZCX2-YW-T001), and the Research Program for Young Scientists at SCSIO

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Fu, D., Zhang, Y. & Yu, Z. Cloning and expression analysis of a ubiquitin gene (Ub L40 ) in the haemocytes of Crassostrea hongkongensis under bacterial challenge. Chin. J. Ocean. Limnol. 29, 80–86 (2011). https://doi.org/10.1007/s00343-011-9090-1

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  • DOI: https://doi.org/10.1007/s00343-011-9090-1

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