Abstract
A cDNA clone specific for rat ribosomal protein S11 was isolated by hybrid-selected translation from the cDNA library made for 8-9 S poly(A) RNA from regenerating rat liver. Since this cDNA had not enough length, another clone was selected by colony hybridization using a fragment of isolated cDNA as a probe. The nucleotide sequence of the cDNA was determined. The sequence contains 2 base pairs from the 5' noncoding region, the entire coding region of 477 base pairs, and the 3' noncoding region of 55 base pairs besides the poly(A) tail. The primary structure of the protein S11 was deduced from the nucleotide sequence. It consists of 157 amino acids. Its molecular weight is 18,299. The calculated amino acid composition is consistent with the reported composition of S11 determined on the protein hydrolysate. The amino acid sequence showed a marked homology with that of S16 of Halobacterium cutirubrum and an appreciable homology with that of S17 of Escherichia coli.
Highlights
A cDNA clone specific for rat ribosomal protein S11 shown tobe specific for ribosomal protein S11, andtheir was isolated by hybrid-selected translation from the nucleotidesequences were determined
S 11 was deduced fromthe nucleotide sequence. It con- was copied into cDNA,which was made doublestranded
Its functional implication is not known, shortness of the 3' noncoding sequence seems to be the common feature of the eukaryotic ribosomal protein messenger RNA (13, 28, 29)
Summary
A cDNA clone specific for rat ribosomal protein S11 shown tobe specific for ribosomal protein S11, andtheir was isolated by hybrid-selected translation from the nucleotidesequences were determined. The nucleotide sequence of the cDNA was determined. The primary structure of the protein cDNA-The 8-9 S poly(A) RNA from regenerating rat liver
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