Molecular characterization of the cell cycle-regulated thymidylate synthase gene of Saccharomyces cerevisiae
The complete nucleotide sequence of a 1.8-kilobase DNA fragment containing the cell cycle-regulated thymidylate synthase gene (TMP 1) of the yeast Saccharomyces cerevisiae is presented. This analysis has revealed a 912-base pair open reading frame which encodes a 304-amino acid residue protein with...
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| Veröffentlicht in: | The Journal of biological chemistry 1987-04, Vol.262 (11), p.5298-5307 |
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| container_title | The Journal of biological chemistry |
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| creator | Taylor, G.R. Lagosky, P.A. Storms, R.K. Haynes, R.H. |
| description | The complete nucleotide sequence of a 1.8-kilobase DNA fragment containing the cell cycle-regulated thymidylate synthase gene (TMP 1) of the yeast Saccharomyces cerevisiae is presented. This analysis has revealed a 912-base pair open reading frame which encodes a 304-amino acid residue protein with a calculated Mr of 35,007. The tmp1-6 and cdc21-1 mutant alleles of this gene also have been sequenced, and both show single base pair changes which would result in different amino acid substitutions. The amino acid sequence of the yeast thymidylate synthase gene derived from the DNA sequence shows considerable homology when compared with the human, mouse, Herpesvirus saimiri, Leishmania major, Leishmania tropica, Escherichia coli, Lactobacillus casei, bacteriophage T4, and Bacillus subtilis phage phi 3T enzymes. Northern blot hybridization reveals that the TMP 1 mRNA is a 1.15-kilobase polyadenylated transcript. A set of consensus yeast mRNA splice sequences appears within the open reading frame of TMP 1, but S1 nuclease protection experiments reveal that splicing of the mRNA does not occur. Disruption of the gene by the introduction of a large insertion did not produce any defect besides the expected dependence on dTMP for growth. Specifically, the viability of the mutants in the presence of dTMP indicates that the protein does not play a significant structural role in a complex of replication enzymes. |
| doi_str_mv | 10.1016/S0021-9258(18)61188-3 |
| format | Article |
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This analysis has revealed a 912-base pair open reading frame which encodes a 304-amino acid residue protein with a calculated Mr of 35,007. The tmp1-6 and cdc21-1 mutant alleles of this gene also have been sequenced, and both show single base pair changes which would result in different amino acid substitutions. The amino acid sequence of the yeast thymidylate synthase gene derived from the DNA sequence shows considerable homology when compared with the human, mouse, Herpesvirus saimiri, Leishmania major, Leishmania tropica, Escherichia coli, Lactobacillus casei, bacteriophage T4, and Bacillus subtilis phage phi 3T enzymes. Northern blot hybridization reveals that the TMP 1 mRNA is a 1.15-kilobase polyadenylated transcript. A set of consensus yeast mRNA splice sequences appears within the open reading frame of TMP 1, but S1 nuclease protection experiments reveal that splicing of the mRNA does not occur. Disruption of the gene by the introduction of a large insertion did not produce any defect besides the expected dependence on dTMP for growth. Specifically, the viability of the mutants in the presence of dTMP indicates that the protein does not play a significant structural role in a complex of replication enzymes.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)61188-3</identifier><identifier>PMID: 3031048</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>ACIDE AMINE ; ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; Alleles ; Amino Acid Sequence ; AMINO ACIDS ; AMINOACIDOS ; Base Sequence ; Biological and medical sciences ; Cell Cycle ; Cloning, Molecular ; DNA, Fungal - analysis ; Endonucleases - metabolism ; ENZYMIC ACTIVITY ; Fundamental and applied biological sciences. Psychology ; genes ; Genes. Genome ; Molecular and cellular biology ; Molecular genetics ; mutants ; Nucleic Acid Hybridization ; NUCLEOTIDE ; nucleotide sequence ; NUCLEOTIDES ; NUCLEOTIDOS ; point mutation ; SACCHAROMYCES CEREVISIAE ; Saccharomyces cerevisiae - enzymology ; Saccharomyces cerevisiae - genetics ; Single-Strand Specific DNA and RNA Endonucleases ; thymidylate synthase ; Thymidylate Synthase - genetics</subject><ispartof>The Journal of biological chemistry, 1987-04, Vol.262 (11), p.5298-5307</ispartof><rights>1987 © 1987 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c514t-b2bfe5080a928dd8ff2cf37c6eb12cb0f06b550d87dfa880a609c710623f9e833</citedby><cites>FETCH-LOGICAL-c514t-b2bfe5080a928dd8ff2cf37c6eb12cb0f06b550d87dfa880a609c710623f9e833</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7407656$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3031048$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Taylor, G.R.</creatorcontrib><creatorcontrib>Lagosky, P.A.</creatorcontrib><creatorcontrib>Storms, R.K.</creatorcontrib><creatorcontrib>Haynes, R.H.</creatorcontrib><title>Molecular characterization of the cell cycle-regulated thymidylate synthase gene of Saccharomyces cerevisiae</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The complete nucleotide sequence of a 1.8-kilobase DNA fragment containing the cell cycle-regulated thymidylate synthase gene (TMP 1) of the yeast Saccharomyces cerevisiae is presented. This analysis has revealed a 912-base pair open reading frame which encodes a 304-amino acid residue protein with a calculated Mr of 35,007. The tmp1-6 and cdc21-1 mutant alleles of this gene also have been sequenced, and both show single base pair changes which would result in different amino acid substitutions. The amino acid sequence of the yeast thymidylate synthase gene derived from the DNA sequence shows considerable homology when compared with the human, mouse, Herpesvirus saimiri, Leishmania major, Leishmania tropica, Escherichia coli, Lactobacillus casei, bacteriophage T4, and Bacillus subtilis phage phi 3T enzymes. Northern blot hybridization reveals that the TMP 1 mRNA is a 1.15-kilobase polyadenylated transcript. A set of consensus yeast mRNA splice sequences appears within the open reading frame of TMP 1, but S1 nuclease protection experiments reveal that splicing of the mRNA does not occur. Disruption of the gene by the introduction of a large insertion did not produce any defect besides the expected dependence on dTMP for growth. Specifically, the viability of the mutants in the presence of dTMP indicates that the protein does not play a significant structural role in a complex of replication enzymes.</description><subject>ACIDE AMINE</subject><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>Alleles</subject><subject>Amino Acid Sequence</subject><subject>AMINO ACIDS</subject><subject>AMINOACIDOS</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Cell Cycle</subject><subject>Cloning, Molecular</subject><subject>DNA, Fungal - analysis</subject><subject>Endonucleases - metabolism</subject><subject>ENZYMIC ACTIVITY</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>genes</subject><subject>Genes. Genome</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>mutants</subject><subject>Nucleic Acid Hybridization</subject><subject>NUCLEOTIDE</subject><subject>nucleotide sequence</subject><subject>NUCLEOTIDES</subject><subject>NUCLEOTIDOS</subject><subject>point mutation</subject><subject>SACCHAROMYCES CEREVISIAE</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Single-Strand Specific DNA and RNA Endonucleases</subject><subject>thymidylate synthase</subject><subject>Thymidylate Synthase - genetics</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkV-L1DAUxYMo67j6BYSFgiL6UM1N2iZ9Eln8Bys-jAu-hTS9mUbaZjfprNRPb7IzzOvmJYTzOyfccwm5APoeKDQftpQyKFtWy7cg3zUAUpb8EdkAlbzkNfx-TDYn5Cl5FuMfmk7Vwhk545QDreSGjD_8iGY_6lCYQQdtFgzun16cnwtvi2XAwuA4FmY1I5YBdwldsE_COrl-zY8irvMy6IjFDmfMrq02OcxPq8GY_AHvXHQan5MnVo8RXxzvc3L95fOvy2_l1c-v3y8_XZWmhmopO9ZZrKmkumWy76W1zFguTIMdMNNRS5uurmkvRW-1TFhDWyOANozbFiXn5-TNIfcm-Ns9xkVNLuYx9Ix-H5UQVUV51T4IQiUaLiAn1gfQBB9jQKtugpt0WBVQldeh7tehctcKpLpfh8q-i-MH-27C_uQ69p_010ddR6NHG_RsXDxhoqKiqZuEvTpgg9sNf11A1TlvBpwUa5gCUDVrc9jLA2W1V3oXUtD1VgomW5YjPh5ETMXfOQwqGoezwT7FmUX13j0wy39rhLxG</recordid><startdate>19870415</startdate><enddate>19870415</enddate><creator>Taylor, G.R.</creator><creator>Lagosky, P.A.</creator><creator>Storms, R.K.</creator><creator>Haynes, R.H.</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19870415</creationdate><title>Molecular characterization of the cell cycle-regulated thymidylate synthase gene of Saccharomyces cerevisiae</title><author>Taylor, G.R. ; Lagosky, P.A. ; Storms, R.K. ; Haynes, R.H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c514t-b2bfe5080a928dd8ff2cf37c6eb12cb0f06b550d87dfa880a609c710623f9e833</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>ACIDE AMINE</topic><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>Alleles</topic><topic>Amino Acid Sequence</topic><topic>AMINO ACIDS</topic><topic>AMINOACIDOS</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Cell Cycle</topic><topic>Cloning, Molecular</topic><topic>DNA, Fungal - analysis</topic><topic>Endonucleases - metabolism</topic><topic>ENZYMIC ACTIVITY</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>genes</topic><topic>Genes. Genome</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>mutants</topic><topic>Nucleic Acid Hybridization</topic><topic>NUCLEOTIDE</topic><topic>nucleotide sequence</topic><topic>NUCLEOTIDES</topic><topic>NUCLEOTIDOS</topic><topic>point mutation</topic><topic>SACCHAROMYCES CEREVISIAE</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Single-Strand Specific DNA and RNA Endonucleases</topic><topic>thymidylate synthase</topic><topic>Thymidylate Synthase - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Taylor, G.R.</creatorcontrib><creatorcontrib>Lagosky, P.A.</creatorcontrib><creatorcontrib>Storms, R.K.</creatorcontrib><creatorcontrib>Haynes, R.H.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Taylor, G.R.</au><au>Lagosky, P.A.</au><au>Storms, R.K.</au><au>Haynes, R.H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular characterization of the cell cycle-regulated thymidylate synthase gene of Saccharomyces cerevisiae</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1987-04-15</date><risdate>1987</risdate><volume>262</volume><issue>11</issue><spage>5298</spage><epage>5307</epage><pages>5298-5307</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>The complete nucleotide sequence of a 1.8-kilobase DNA fragment containing the cell cycle-regulated thymidylate synthase gene (TMP 1) of the yeast Saccharomyces cerevisiae is presented. This analysis has revealed a 912-base pair open reading frame which encodes a 304-amino acid residue protein with a calculated Mr of 35,007. The tmp1-6 and cdc21-1 mutant alleles of this gene also have been sequenced, and both show single base pair changes which would result in different amino acid substitutions. The amino acid sequence of the yeast thymidylate synthase gene derived from the DNA sequence shows considerable homology when compared with the human, mouse, Herpesvirus saimiri, Leishmania major, Leishmania tropica, Escherichia coli, Lactobacillus casei, bacteriophage T4, and Bacillus subtilis phage phi 3T enzymes. Northern blot hybridization reveals that the TMP 1 mRNA is a 1.15-kilobase polyadenylated transcript. A set of consensus yeast mRNA splice sequences appears within the open reading frame of TMP 1, but S1 nuclease protection experiments reveal that splicing of the mRNA does not occur. Disruption of the gene by the introduction of a large insertion did not produce any defect besides the expected dependence on dTMP for growth. Specifically, the viability of the mutants in the presence of dTMP indicates that the protein does not play a significant structural role in a complex of replication enzymes.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>3031048</pmid><doi>10.1016/S0021-9258(18)61188-3</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| issn | 0021-9258 1083-351X |
| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | ACIDE AMINE ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE Alleles Amino Acid Sequence AMINO ACIDS AMINOACIDOS Base Sequence Biological and medical sciences Cell Cycle Cloning, Molecular DNA, Fungal - analysis Endonucleases - metabolism ENZYMIC ACTIVITY Fundamental and applied biological sciences. Psychology genes Genes. Genome Molecular and cellular biology Molecular genetics mutants Nucleic Acid Hybridization NUCLEOTIDE nucleotide sequence NUCLEOTIDES NUCLEOTIDOS point mutation SACCHAROMYCES CEREVISIAE Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics Single-Strand Specific DNA and RNA Endonucleases thymidylate synthase Thymidylate Synthase - genetics |
| title | Molecular characterization of the cell cycle-regulated thymidylate synthase gene of Saccharomyces cerevisiae |
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