NDLI: Giant panda ribosomal protein S14: cDNA, genomic sequence cloning, sequence analysis, and overexpression.

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Giant panda ribosomal protein S14: cDNA, genomic sequence cloning, sequence analysis, and overexpression.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Zhang, T. Hou, W-R Song, Y. Hou, Y-L Wu, G-F
Description	Country affiliation: China Author Affiliation: Wu GF ( Key Laboratory of Southwest China Wildlife Resources Conservation (Ministry of Education), College of Life Science, China West Normal University, Nanchong, China.)
Abstract	RPS14 is a component of the 40S ribosomal subunit encoded by the RPS14 gene and is required for its maturation. The cDNA and the genomic sequence of RPS14 were cloned successfully from the giant panda (Ailuropoda melanoleuca) using RT-PCR technology and touchdown-PCR, respectively; they were both sequenced and analyzed. The length of the cloned cDNA fragment was 492 bp; it contained an open-reading frame of 456 bp, encoding 151 amino acids. The length of the genomic sequence is 3421 bp; it contains four exons and three introns. Alignment analysis indicates that the nucleotide sequence shares a high degree of homology with those of Homo sapiens, Bos taurus, Mus musculus, Rattus norvegicus, Gallus gallus, Xenopus laevis, and Danio rerio (93.64, 83.37, 92.54, 91.89, 87.28, 84.21, and 84.87%, respectively). Comparison of the deduced amino acid sequences of the giant panda with those of these other species revealed that the RPS14 of giant panda is highly homologous with those of B. taurus, R. norvegicus and D. rerio (85.99, 99.34 and 99.34%, respectively), and is 100% identical with the others. This degree of conservation of RPS14 suggests evolutionary selection. Topology prediction shows that there are two N-glycosylation sites, three protein kinase C phosphorylation sites, two casein kinase II phosphorylation sites, four N-myristoylation sites, two amidation sites, and one ribosomal protein S11 signature in the RPS14 protein of the giant panda. The RPS14 gene can be readily expressed in Escherichia coli. When it was fused with the N-terminally His-tagged protein, it gave rise to accumulation of an expected 22-kDa polypeptide, in good agreement with the predicted molecular weight. The expression product obtained can be purified for studies of its function.
e-ISSN	16765680
Journal	Genetics and Molecular Research
Issue Number	4
Volume Number	9
Language	English
Publisher	Fundação de Pesquisas Científicas de Ribeirão Preto
Publisher Date	2010-10-13
Publisher Place	Brazil
Access Restriction	Open
Subject Keyword	Carnivora Genetics Dna, Complementary Ribosomal Proteins Amino Acid Sequence Animals Cloning, Molecular Dna Primers Escherichia Coli Molecular Sequence Data Reverse Transcriptase Polymerase Chain Reaction Sequence Homology, Amino Acid Research Support, Non-u.s. Gov't Discipline Genetics Discipline Molecular Biology Discipline Bioinformatics
Content Type	Text
Resource Type	Article

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