Sequence comparisons of complementary DNAs encoding aequorin isotypes

Aequorin is the Ca2+-activated photoprotein which participates in the bioluminescence from the circumoral ring of the hydromedusa Aequorea victoria. The nucleotide sequences of five aequorin cDNAs have been compared and shown to code for three aequorin isoforms. The cDNA AEQ1 contains the entire pro...

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Veröffentlicht in:Biochemistry (Easton) 1987-03, Vol.26 (5), p.1326-1332
Hauptverfasser: Prasher, Douglas C, McCann, Richard O, Longiaru, Mathew, Cormier, Milton J
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creator Prasher, Douglas C
McCann, Richard O
Longiaru, Mathew
Cormier, Milton J
description Aequorin is the Ca2+-activated photoprotein which participates in the bioluminescence from the circumoral ring of the hydromedusa Aequorea victoria. The nucleotide sequences of five aequorin cDNAs have been compared and shown to code for three aequorin isoforms. The cDNA AEQ1 contains the entire protein coding region of 196 amino acids. The other four cDNAs contain only 70-90% of the coding region and apparently code for at least two other isoforms whose amino acid sequences differ significantly from that encoded by AEQ1. The nucleotide sequences coding for the three isotypes differ at a minimum of 54 positions out of a total of 588 nucleotides necessary to code for apoaequorin. Of these nucleotide differences, 24 account for 23 amino acid replacements, substantiating the microheterogeneity observed during sequencing of purified native aequorin [Charbonneau, H., Walsh, K.A., McCann, R.O., Prendergast, F.G., Cormier, M.J., & Vanaman, T.C. (1985) Biochemistry 24, 6762-6771]. Comparison of the deduced cDNA translations with the native protein sequences suggests the loss of seven residues from the amino terminus during purification of aequorin from Aequorea. Aequorin rapidly extracted from the jellyfish using conditions to minimize proteolysis is shown to have a larger molecular weight than that of purified native aequorin. Escherichia coli expressed aequorin encoded by AEQ1 is shown to have the same molecular weight and isoelectric point as those of one of the isotypes rapidly extracted from Aequorea.
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The nucleotide sequences of five aequorin cDNAs have been compared and shown to code for three aequorin isoforms. The cDNA AEQ1 contains the entire protein coding region of 196 amino acids. The other four cDNAs contain only 70-90% of the coding region and apparently code for at least two other isoforms whose amino acid sequences differ significantly from that encoded by AEQ1. The nucleotide sequences coding for the three isotypes differ at a minimum of 54 positions out of a total of 588 nucleotides necessary to code for apoaequorin. Of these nucleotide differences, 24 account for 23 amino acid replacements, substantiating the microheterogeneity observed during sequencing of purified native aequorin [Charbonneau, H., Walsh, K.A., McCann, R.O., Prendergast, F.G., Cormier, M.J., &amp; Vanaman, T.C. (1985) Biochemistry 24, 6762-6771]. Comparison of the deduced cDNA translations with the native protein sequences suggests the loss of seven residues from the amino terminus during purification of aequorin from Aequorea. Aequorin rapidly extracted from the jellyfish using conditions to minimize proteolysis is shown to have a larger molecular weight than that of purified native aequorin. Escherichia coli expressed aequorin encoded by AEQ1 is shown to have the same molecular weight and isoelectric point as those of one of the isotypes rapidly extracted from Aequorea.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00379a019</identifier><identifier>PMID: 2882777</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Aequorea victoria ; aequorin ; Aequorin - genetics ; amino acid sequence ; amino acids ; Apoproteins - genetics ; Base Sequence ; Biological and medical sciences ; bioluminescence ; cDNA ; Cnidaria - genetics ; DNA ; DNA - genetics ; Escherichia coli ; Fundamental and applied biological sciences. Psychology ; Genes. 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The nucleotide sequences of five aequorin cDNAs have been compared and shown to code for three aequorin isoforms. The cDNA AEQ1 contains the entire protein coding region of 196 amino acids. The other four cDNAs contain only 70-90% of the coding region and apparently code for at least two other isoforms whose amino acid sequences differ significantly from that encoded by AEQ1. The nucleotide sequences coding for the three isotypes differ at a minimum of 54 positions out of a total of 588 nucleotides necessary to code for apoaequorin. Of these nucleotide differences, 24 account for 23 amino acid replacements, substantiating the microheterogeneity observed during sequencing of purified native aequorin [Charbonneau, H., Walsh, K.A., McCann, R.O., Prendergast, F.G., Cormier, M.J., &amp; Vanaman, T.C. (1985) Biochemistry 24, 6762-6771]. Comparison of the deduced cDNA translations with the native protein sequences suggests the loss of seven residues from the amino terminus during purification of aequorin from Aequorea. Aequorin rapidly extracted from the jellyfish using conditions to minimize proteolysis is shown to have a larger molecular weight than that of purified native aequorin. Escherichia coli expressed aequorin encoded by AEQ1 is shown to have the same molecular weight and isoelectric point as those of one of the isotypes rapidly extracted from Aequorea.</description><subject>Aequorea victoria</subject><subject>aequorin</subject><subject>Aequorin - genetics</subject><subject>amino acid sequence</subject><subject>amino acids</subject><subject>Apoproteins - genetics</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>bioluminescence</subject><subject>cDNA</subject><subject>Cnidaria - genetics</subject><subject>DNA</subject><subject>DNA - genetics</subject><subject>Escherichia coli</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes. Genome</subject><subject>Isoelectric Point</subject><subject>Luminescent Proteins - genetics</subject><subject>Marine</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Weight</subject><subject>nucleotide sequence</subject><subject>nucleotides</subject><subject>proteins</subject><subject>Sequence Homology, Nucleic Acid</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0M9rFDEUB_AgSl1bT56FOYg9yOjL5MebHEutbqVooVW8hWzmRabOTLbJLLT_vWl3WTwInsLjffLy8mXsFYf3HBr-YdUDCDQOuHnCFlw1UEtj1FO2AABdN0bDc_Yi55tSSkB5wA6atm0QccHOruh2Q5Onysdx7VKf45SrGB7LgUaaZpfuq49fT3JVWOz66Vflyp2Y-qkqer5fUz5iz4IbMr3cnYfs-6ez69NlffHt8_npyUXtJJdzHQR5IgPkvEfOBRfaa2m80IBt6LRXwegueEUogkHdhLDqOpBa8a5BUOKQvd3OXadY1s6zHfvsaRjcRHGTLaLUgkv4L-QSFbZCF_huC32KOScKdp36sXzZcrAP6dq_0i369W7sZjVSt7e7OEv_za7vsndDSG7yfd4zlIIr_vBovWV9nulu33bpt9UoUNnryyv7s_3yYymapW2LP95657O9iZs0lZD_ueAfFyCdDQ</recordid><startdate>19870310</startdate><enddate>19870310</enddate><creator>Prasher, Douglas C</creator><creator>McCann, Richard O</creator><creator>Longiaru, Mathew</creator><creator>Cormier, Milton J</creator><general>American Chemical Society</general><scope>BSCLL</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>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>L.G</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19870310</creationdate><title>Sequence comparisons of complementary DNAs encoding aequorin isotypes</title><author>Prasher, Douglas C ; McCann, Richard O ; Longiaru, Mathew ; Cormier, Milton J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a414t-f3ecee90eacc7113136c649c36078fd6c5f96dfc5e73f9762ffbdd04651d27053</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Aequorea victoria</topic><topic>aequorin</topic><topic>Aequorin - genetics</topic><topic>amino acid sequence</topic><topic>amino acids</topic><topic>Apoproteins - genetics</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>bioluminescence</topic><topic>cDNA</topic><topic>Cnidaria - genetics</topic><topic>DNA</topic><topic>DNA - genetics</topic><topic>Escherichia coli</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes. Genome</topic><topic>Isoelectric Point</topic><topic>Luminescent Proteins - genetics</topic><topic>Marine</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Weight</topic><topic>nucleotide sequence</topic><topic>nucleotides</topic><topic>proteins</topic><topic>Sequence Homology, Nucleic Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Prasher, Douglas C</creatorcontrib><creatorcontrib>McCann, Richard O</creatorcontrib><creatorcontrib>Longiaru, Mathew</creatorcontrib><creatorcontrib>Cormier, Milton J</creatorcontrib><collection>Istex</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>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>Aquatic Science &amp; Fisheries Abstracts (ASFA) 1: Biological Sciences &amp; Living Resources</collection><collection>Aquatic Science &amp; Fisheries Abstracts (ASFA) Professional</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Prasher, Douglas C</au><au>McCann, Richard O</au><au>Longiaru, Mathew</au><au>Cormier, Milton J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Sequence comparisons of complementary DNAs encoding aequorin isotypes</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1987-03-10</date><risdate>1987</risdate><volume>26</volume><issue>5</issue><spage>1326</spage><epage>1332</epage><pages>1326-1332</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>Aequorin is the Ca2+-activated photoprotein which participates in the bioluminescence from the circumoral ring of the hydromedusa Aequorea victoria. The nucleotide sequences of five aequorin cDNAs have been compared and shown to code for three aequorin isoforms. The cDNA AEQ1 contains the entire protein coding region of 196 amino acids. The other four cDNAs contain only 70-90% of the coding region and apparently code for at least two other isoforms whose amino acid sequences differ significantly from that encoded by AEQ1. The nucleotide sequences coding for the three isotypes differ at a minimum of 54 positions out of a total of 588 nucleotides necessary to code for apoaequorin. Of these nucleotide differences, 24 account for 23 amino acid replacements, substantiating the microheterogeneity observed during sequencing of purified native aequorin [Charbonneau, H., Walsh, K.A., McCann, R.O., Prendergast, F.G., Cormier, M.J., &amp; Vanaman, T.C. (1985) Biochemistry 24, 6762-6771]. Comparison of the deduced cDNA translations with the native protein sequences suggests the loss of seven residues from the amino terminus during purification of aequorin from Aequorea. Aequorin rapidly extracted from the jellyfish using conditions to minimize proteolysis is shown to have a larger molecular weight than that of purified native aequorin. Escherichia coli expressed aequorin encoded by AEQ1 is shown to have the same molecular weight and isoelectric point as those of one of the isotypes rapidly extracted from Aequorea.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>2882777</pmid><doi>10.1021/bi00379a019</doi><tpages>7</tpages></addata></record>
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subjects Aequorea victoria
aequorin
Aequorin - genetics
amino acid sequence
amino acids
Apoproteins - genetics
Base Sequence
Biological and medical sciences
bioluminescence
cDNA
Cnidaria - genetics
DNA
DNA - genetics
Escherichia coli
Fundamental and applied biological sciences. Psychology
Genes. Genome
Isoelectric Point
Luminescent Proteins - genetics
Marine
Molecular and cellular biology
Molecular genetics
Molecular Weight
nucleotide sequence
nucleotides
proteins
Sequence Homology, Nucleic Acid
title Sequence comparisons of complementary DNAs encoding aequorin isotypes
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