The Isolation and Analysis of Rubber Elongation Factor Gene and Its 5′-End Promoter Region
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Rubber Elongation Factor, a major protein in the latex of rubber trees, is one of the most important enzymes in rubber biosynthesis. The cDNA of rubber elongation factor gene was cloned by the method of RT PCR and sequenced. The REF cDNA coding region consists of 414 bp encoding 138 amino acids with a 3′ non coding region of 112bp. Both the nucleotide sequences and the amino acid sequences of the coding region have 100% homology with the REF cDNA sequences reported by Goyvaerts E et al. The nucleotide sequence of the 3′ non coding region have 98% homology with the latter. Then, the 5′ end sequence of the promoter region of this gene with the length of 260bp has also been isolated by the method of chromosome walking. The sequence includes typical TATA box and CAAT box. The expression of the Rubber Elongation Factor gene in the latex and in the leaf has been detected by Northern blot. The preliminary results show the Rubber Elongation Factor expresses principally in latex.Keywords:
Elongation factor
Coding region
Homology
Elongation
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A cDNA clone specific for rat ribosomal protein S 11 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 S 11 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 S l l 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.
Ribosomal protein
Sequence (biology)
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Journal Article Dynamic Aspects in the Expression of the Goat Insulin-like Growth Factor-I (IGF-I) Gene: Diversity in Transcription and Post-transcription Get access Satoshi Mikawa, Satoshi Mikawa Laboratory of Biochemistry, Department of Agricultural Chemistry, Kyoto University, Kyoto 606-01, Japan Search for other works by this author on: Oxford Academic Google Scholar Gen-ichi Yoshikawa, Gen-ichi Yoshikawa Laboratory of Biochemistry, Department of Agricultural Chemistry, Kyoto University, Kyoto 606-01, Japan Search for other works by this author on: Oxford Academic Google Scholar Hideyuki Aoki, Hideyuki Aoki Laboratory of Biochemistry, Department of Agricultural Chemistry, Kyoto University, Kyoto 606-01, Japan Search for other works by this author on: Oxford Academic Google Scholar Yoshiaki Yamano, Yoshiaki Yamano Laboratory of Biochemistry, Department of Agricultural Chemistry, Kyoto University, Kyoto 606-01, Japan Present address: Faculty of Agriculture, Tottori University, Tottori 680, Japan. Search for other works by this author on: Oxford Academic Google Scholar Hiroshi Sakai, Hiroshi Sakai Laboratory of Biochemistry, Department of Agricultural Chemistry, Kyoto University, Kyoto 606-01, Japan Search for other works by this author on: Oxford Academic Google Scholar Tohru Komano Tohru Komano Laboratory of Biochemistry, Department of Agricultural Chemistry, Kyoto University, Kyoto 606-01, Japan Corresponding author. Search for other works by this author on: Oxford Academic Google Scholar Bioscience, Biotechnology, and Biochemistry, Volume 59, Issue 1, 1 January 1995, Pages 87–92, https://doi.org/10.1271/bbb.59.87 Published: 01 January 1995 Article history Received: 10 August 1994 Published: 01 January 1995
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Homology
Protein primary structure
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A cDNA clone related to lipid transportation and metabolism was isolated by screening subtracted latex cDNA library.According to its sequences information,a novel full-length cDNA termed R28(GenBank number:AY461413) was obtained by using rapid amplification of cDNA ends(RACE).R28 was 1 365 bp long containing a 1 149-bp ORF,flanked by a 96-bp 5'-UTR and a 128-bp 3'-UTR.It encoded 382 amino acids with a theoretical molecular weight of 43.5 kDa and an isoelectric point of 8.97.Hydropathy and transmembrane motif analysis of deduced amino acid sequences indicated that R28 possessed a transmembrane spanning do-main(185-215 aa),and contained a cleaved signal peptide(1-17 aa).The result of the conserved domains analysis indicated that R28 not only has a highly conserved region of acyl-CoA reductase,but also contains a male sterility protein C-terminal region.Multialignment revealed that R28 is the most closely related to the jojoba acyl CoA reductase.
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A complementary DNA clone for the human U1 snRNP-specific C protein has been isolated. The nucleotide sequence of the 733 bp cDNA insert includes a 15 bp 5′-untranslated region, an open reading frame of 477 bp corresponding to 159 amino acids (M r -17, 373 D), and a 223 bp 3′-untranslated region. The identity of the clone was confirmed by in vitro translation of hybrid-selected mRNA or an RNA transcript synthesized from the cDNA. The in vitro synthesized C protein has a slightly greater mobility on SDS-polyacrylamide gels, indicating that the in vivo product is post-translationally modified. The deduced primary structure contains a segment of high proline and methionine content. A region homologous to the RNP consensus sequence, found in the other two U1 snRNP-specific proteins 70K and A, is absent. Analysis of genomic DNA restriction enzyme digests shows hybridizing fragments in the genome of all vertebrate classes. The results are consistent with multicopy representation of the C protein gene in mammals, whereas in the other vertebrate classes the related protein seems to be encoded by a single-copy gene.
snRNP
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Two cDNAs (pLM3c 4.1 and pLM3c 6.1) coding for rabbit cytochrome P450 3c were sequenced. cDNA 4.1 (1768 bp) exhibits an open reading frame from nucleotides 74 to 1576 encoding the 501 amino acid residues of the entire protein. cDNA 6.1 (189 bp) appears to encode the last 24 amino acids. Comparative amino acid sequence analysis indicated that P450 PCN1, PCN2, and HLp from rat and man, were 70, 67, and 73% homologous, respectively, to P450 3c. According to the cytochrome P450 nomenclature, the P450 3c gene is termed P450IIIA4. Comparison of the nucleotide sequences indicated that cDNA 6.1 was 100% homologous to cDNA 4.1. However, whereas a poly(A) tract started 23 nucleotides after the AATAAA consensus sequence in cDNA 6.1, cDNA 4.1 had a 3′ untranslated region extending 101 bp beyond the polyadenylation signal, which lacked poly(A). This observation is consistent with the previous finding that both cDNA 4.1 and 6.1 hybridized with two distinct species of poly(A)RNA (1700 and 1850 bases) from rabbit liver. The extreme 3′-end 79-bp fragment of cDNA 4.1 therefore was isolated by subcloning in pUC12 (clone p18-Rsa I) and used to probe Northern blots of poly(A)RNA from control and rifampicin-treated rabbit liver. In contrast to cDNA 4.1 and 6.1, p18-Rsa I cDNA hybridized only with the largest (1850 bases) mRNA species. We conclude that rabbit liver contains two P450 3c mRNA species differing in the length of their 3′ untranslated region.
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The nucleotide sequence of mRNA for rat cerebellar spot 35 protein, a Ca-binding protein, was determined from recombinant complementary DNA (cDNA) clones. The sequence was composed of 1,714 base pairs (bp) which included the 783 bp of the complete coding region, the 130 bp of the 5'-noncoding region, and the 801 bp of the 3'-noncoding region containing a polyadenylation signal. In addition, a polyadenylic acid [poly(A)] tail was also found. Because the size of spot 35 mRNA was estimated to be about 1,900 bases by Northern blot analysis, the longest insert was verified to contain a nearly full-length cDNA sequence including the poly(A) tail. The amino acid sequence of the protein deduced from the nucleotide sequence contains 261 amino acids and at least five Ca-binding domains. There was a high homology in the amino acid sequences (79%) and the nucleotide sequences (77%) between spot 35 protein and chick intestinal Ca-binding protein (28K).
Coding region
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cDNA clones specific for rat ribosomal protein L5, which is the protein moiety of 5S RNA protein particles, were isolated by using a mixture of tetradecamer deoxyribonucleotide probes reflecting the amino acid sequence of the N-terminal portion of L5. A cDNA clone (pRL5-1) lacking the 3'-terminal region of L5 was isolated by hybrid-selected translation and shown to be L5-specific by the identity of the deduced amino acid sequence and that of the N-terminus of protein L5. pRL5-1 was then used to select another clone (pRL5-2) by colony hybridization which contained the entire coding region, 3'-non-coding region and poly(A) addition signal. The nucleotide sequence of L5-specific cDNA was determined by using these two clones. It contained a total of 1069 base pairs: 123 base pairs in the 5'-non-coding region, 894 base pairs in the coding region and 52 base pairs in the 3'-non-coding region. The poly(A) addition signal appeared at the 33rd nucleotide after the termination codon. The amino acid sequence deduced from this nucleotide sequence consists of 296 amino acids. The homology of amino acid sequence between L5 and other 5S RNA-binding proteins is discussed.
Coding region
Ribosomal protein
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ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTcDNA structure of murine C4b-binding protein, a regulatory component of the serum complement systemTorsten Kristensen, Ronald T. Ogata, L. Ping Chung, Kenneth B. M. Reid, and Brian F. TackCite this: Biochemistry 1987, 26, 15, 4668–4674Publication Date (Print):July 28, 1987Publication History Published online1 May 2002Published inissue 28 July 1987https://pubs.acs.org/doi/10.1021/bi00389a012https://doi.org/10.1021/bi00389a012research-articleACS PublicationsRequest reuse permissionsArticle Views51Altmetric-Citations37LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts
Complement
Component (thermodynamics)
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