Nucleotide sequence of ub52 from the cnidarian Acropora millepora reveals high evolutionary conservation.
We report the cDNA sequence encoding Ub52 from the cnidarian Acropora millepora. As in other eukaryotes, the N-terminal region of the deduced amino-acid sequence is a ubiquitin moiety and the C-terminal region CEP52, a protein component of the large ribosomal subunit. A millepora Ub52 is highly homologous (> 95% identical) with the corresponding Drosophila and vertebrate sequences, the cnidarian sequence having higher identity with these 'higher' metazoan homologs than does the corresponding Caenorhabditis elegans protein. However, the cnidarian sequence contains two unique substitutions in the ubiquitin moiety, Ser22 and Thr28. Northern analysis indicates that A. millepora Ub52 is encoded by a small (< 800 nt) mRNA present in eggs and is first expressed after the early gastrula stage in embryonic development.
Berghammer
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Department of Biochemistry and Molecular Biology, James Cook University of North Queensland, Townsville, Australia.
Hayward
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D
Harrison
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Miller
D J
DJ
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D003063:Cnidaria / Q000235:genetics*; D019143:Evolution, Molecular; D015870:Gene Expression; D008969:Molecular Sequence Data; D011506:Proteins / Q000235:genetics*; D012333:RNA, Messenger; D012269:Ribosomal Proteins
D011506:Proteins; D012333:RNA, Messenger; D012269:Ribosomal Proteins; C102269:Ub52 protein, Acropora millepora