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Isolation of genes encoding the Neurospora vacuolar ATPase. Analysis of vma-1 encoding the 67-kDa subunit reveals homology to other ATPases
The vacuolar membrane of Neurospora crassa contains a H+-translocating ATPase composed of at least three subunits with approximate molecular weights of 70,000, 60,000, and 15,000. Both genomic and cDNA clones encoding the largest subunit, which appears to contain the active site of the enzyme, have...
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Published in: | The Journal of biological chemistry 1988-10, Vol.263 (28), p.13994-14001 |
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creator | Bowman, E J Tenney, K Bowman, B J |
description | The vacuolar membrane of Neurospora crassa contains a H+-translocating ATPase composed of at least three subunits with approximate molecular weights of 70,000, 60,000, and 15,000. Both genomic and cDNA clones encoding the largest subunit, which appears to contain the active site of the enzyme, have been isolated and sequenced. The gene for this subunit, designated vma-1, contains six small introns (60-131 base pairs) and encodes a hydrophilic protein of 607 amino acids, Mr 67,121. Within the sequence is a putative nucleotide-binding region, consistent with the proposal that this subunit contains the site of ATP hydrolysis. This 67-kDa polypeptide shows high homology (62% identical residues overall and 84% in the middle of the protein) to the analogous polypeptide of a higher plant vacuolar ATPase. The hypothesis that the vacuolar ATPase is related to F0F1 ATPases is strongly supported by the finding of considerable homology between the 67-kDa subunit of the Neurospora vacuolar ATPase and both the alpha and beta subunits of F0F1 ATPases. |
doi_str_mv | 10.1016/S0021-9258(18)68175-X |
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Analysis of vma-1 encoding the 67-kDa subunit reveals homology to other ATPases</title><source>ScienceDirect (Online service)</source><creator>Bowman, E J ; Tenney, K ; Bowman, B J</creator><creatorcontrib>Bowman, E J ; Tenney, K ; Bowman, B J</creatorcontrib><description>The vacuolar membrane of Neurospora crassa contains a H+-translocating ATPase composed of at least three subunits with approximate molecular weights of 70,000, 60,000, and 15,000. Both genomic and cDNA clones encoding the largest subunit, which appears to contain the active site of the enzyme, have been isolated and sequenced. The gene for this subunit, designated vma-1, contains six small introns (60-131 base pairs) and encodes a hydrophilic protein of 607 amino acids, Mr 67,121. Within the sequence is a putative nucleotide-binding region, consistent with the proposal that this subunit contains the site of ATP hydrolysis. This 67-kDa polypeptide shows high homology (62% identical residues overall and 84% in the middle of the protein) to the analogous polypeptide of a higher plant vacuolar ATPase. The hypothesis that the vacuolar ATPase is related to F0F1 ATPases is strongly supported by the finding of considerable homology between the 67-kDa subunit of the Neurospora vacuolar ATPase and both the alpha and beta subunits of F0F1 ATPases.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)68175-X</identifier><identifier>PMID: 2971651</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Adenosine Triphosphatases - genetics ; Amino Acid Sequence ; Base Sequence ; Biological and medical sciences ; CHAMPIGNON ; CODE GENETIQUE ; CODIGO GENETICO ; DNA, Fungal - genetics ; DNA, Fungal - isolation & purification ; Fundamental and applied biological sciences. Psychology ; FUNGI ; Genes ; Genes, Fungal ; Genes. Genome ; GENETIC CODE ; HIDROLASAS ; HYDROLASE ; HYDROLASES ; Macromolecular Substances ; Molecular and cellular biology ; Molecular genetics ; Molecular Sequence Data ; Molecular Weight ; Neurospora - genetics ; NEUROSPORA CRASSA ; Neurospora crassa - enzymology ; Neurospora crassa - genetics ; NUCLEOTIDE ; NUCLEOTIDES ; NUCLEOTIDOS ; VACUOLA ; VACUOLE ; VACUOLES ; Vacuoles - enzymology</subject><ispartof>The Journal of biological chemistry, 1988-10, Vol.263 (28), p.13994-14001</ispartof><rights>1988 © 1988 ASBMB. 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Analysis of vma-1 encoding the 67-kDa subunit reveals homology to other ATPases</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The vacuolar membrane of Neurospora crassa contains a H+-translocating ATPase composed of at least three subunits with approximate molecular weights of 70,000, 60,000, and 15,000. Both genomic and cDNA clones encoding the largest subunit, which appears to contain the active site of the enzyme, have been isolated and sequenced. The gene for this subunit, designated vma-1, contains six small introns (60-131 base pairs) and encodes a hydrophilic protein of 607 amino acids, Mr 67,121. Within the sequence is a putative nucleotide-binding region, consistent with the proposal that this subunit contains the site of ATP hydrolysis. This 67-kDa polypeptide shows high homology (62% identical residues overall and 84% in the middle of the protein) to the analogous polypeptide of a higher plant vacuolar ATPase. The hypothesis that the vacuolar ATPase is related to F0F1 ATPases is strongly supported by the finding of considerable homology between the 67-kDa subunit of the Neurospora vacuolar ATPase and both the alpha and beta subunits of F0F1 ATPases.</description><subject>Adenosine Triphosphatases - genetics</subject><subject>Amino Acid Sequence</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>CHAMPIGNON</subject><subject>CODE GENETIQUE</subject><subject>CODIGO GENETICO</subject><subject>DNA, Fungal - genetics</subject><subject>DNA, Fungal - isolation & purification</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>FUNGI</subject><subject>Genes</subject><subject>Genes, Fungal</subject><subject>Genes. Genome</subject><subject>GENETIC CODE</subject><subject>HIDROLASAS</subject><subject>HYDROLASE</subject><subject>HYDROLASES</subject><subject>Macromolecular Substances</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Neurospora - genetics</subject><subject>NEUROSPORA CRASSA</subject><subject>Neurospora crassa - enzymology</subject><subject>Neurospora crassa - genetics</subject><subject>NUCLEOTIDE</subject><subject>NUCLEOTIDES</subject><subject>NUCLEOTIDOS</subject><subject>VACUOLA</subject><subject>VACUOLE</subject><subject>VACUOLES</subject><subject>Vacuoles - enzymology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><recordid>eNqFkUFv1DAQhSMEKkvhDyBV8gEhOKR4kthxTmhVClSqAKmttDdr4kx2DUm82MlW-xv403i7yyJO-OLDfO-N5r0kOQN-DhzkuxvOM0irTKg3oN5KBaVIF4-SGXCVp7mAxeNkdkSeJs9C-M7jKyo4SU6yqgQpYJb8ugquw9G6gbmWLWmgwGgwrrHDko0rYl9o8i6snUe2QTNF2LP57TcMdM7mA3bbYMNOuukxhX-lskx_fEAWpnoa7Mg8bQi7wFaud51bbtnomIvcH7_wPHnSRoBeHP7T5O7j5e3F5_T666eri_l1aoTgYwooVCWxrmXZEOZNy4ELrlA2nLAWKjdVXgopK2oVN0ULsi4qgbwElEVZq_w0eb33XXv3c6Iw6t4GQ12HA7kpaBBQQJ7LCIo9aGIEwVOr19726LcauN6VoB9K0LuENSj9UIJeRN3ZYcFU99QcVYfU4_zVYY7BYNd6HIwNR6zkikOV_8VWdrm6t550bZ1ZUa8zmessrsyrqojYyz3WotO49NHp7kYpmZXlzuP9fkgx0I0lr4OxsSVqop8ZdePsf475De6SuC0</recordid><startdate>19881005</startdate><enddate>19881005</enddate><creator>Bowman, E J</creator><creator>Tenney, K</creator><creator>Bowman, B J</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>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>19881005</creationdate><title>Isolation of genes encoding the Neurospora vacuolar ATPase. Analysis of vma-1 encoding the 67-kDa subunit reveals homology to other ATPases</title><author>Bowman, E J ; Tenney, K ; Bowman, B J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c550t-1a5896abb67dea3df010508a6d0eab583c9375669ef80c4f16b495a071a647b83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Adenosine Triphosphatases - genetics</topic><topic>Amino Acid Sequence</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>CHAMPIGNON</topic><topic>CODE GENETIQUE</topic><topic>CODIGO GENETICO</topic><topic>DNA, Fungal - genetics</topic><topic>DNA, Fungal - isolation & purification</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>FUNGI</topic><topic>Genes</topic><topic>Genes, Fungal</topic><topic>Genes. Genome</topic><topic>GENETIC CODE</topic><topic>HIDROLASAS</topic><topic>HYDROLASE</topic><topic>HYDROLASES</topic><topic>Macromolecular Substances</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Neurospora - genetics</topic><topic>NEUROSPORA CRASSA</topic><topic>Neurospora crassa - enzymology</topic><topic>Neurospora crassa - genetics</topic><topic>NUCLEOTIDE</topic><topic>NUCLEOTIDES</topic><topic>NUCLEOTIDOS</topic><topic>VACUOLA</topic><topic>VACUOLE</topic><topic>VACUOLES</topic><topic>Vacuoles - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bowman, E J</creatorcontrib><creatorcontrib>Tenney, K</creatorcontrib><creatorcontrib>Bowman, B J</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>Nucleic Acids Abstracts</collection><collection>Technology Research Database</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><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bowman, E J</au><au>Tenney, K</au><au>Bowman, B J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Isolation of genes encoding the Neurospora vacuolar ATPase. Analysis of vma-1 encoding the 67-kDa subunit reveals homology to other ATPases</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1988-10-05</date><risdate>1988</risdate><volume>263</volume><issue>28</issue><spage>13994</spage><epage>14001</epage><pages>13994-14001</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>The vacuolar membrane of Neurospora crassa contains a H+-translocating ATPase composed of at least three subunits with approximate molecular weights of 70,000, 60,000, and 15,000. Both genomic and cDNA clones encoding the largest subunit, which appears to contain the active site of the enzyme, have been isolated and sequenced. The gene for this subunit, designated vma-1, contains six small introns (60-131 base pairs) and encodes a hydrophilic protein of 607 amino acids, Mr 67,121. Within the sequence is a putative nucleotide-binding region, consistent with the proposal that this subunit contains the site of ATP hydrolysis. This 67-kDa polypeptide shows high homology (62% identical residues overall and 84% in the middle of the protein) to the analogous polypeptide of a higher plant vacuolar ATPase. The hypothesis that the vacuolar ATPase is related to F0F1 ATPases is strongly supported by the finding of considerable homology between the 67-kDa subunit of the Neurospora vacuolar ATPase and both the alpha and beta subunits of F0F1 ATPases.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>2971651</pmid><doi>10.1016/S0021-9258(18)68175-X</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Adenosine Triphosphatases - genetics Amino Acid Sequence Base Sequence Biological and medical sciences CHAMPIGNON CODE GENETIQUE CODIGO GENETICO DNA, Fungal - genetics DNA, Fungal - isolation & purification Fundamental and applied biological sciences. Psychology FUNGI Genes Genes, Fungal Genes. Genome GENETIC CODE HIDROLASAS HYDROLASE HYDROLASES Macromolecular Substances Molecular and cellular biology Molecular genetics Molecular Sequence Data Molecular Weight Neurospora - genetics NEUROSPORA CRASSA Neurospora crassa - enzymology Neurospora crassa - genetics NUCLEOTIDE NUCLEOTIDES NUCLEOTIDOS VACUOLA VACUOLE VACUOLES Vacuoles - enzymology |
title | Isolation of genes encoding the Neurospora vacuolar ATPase. Analysis of vma-1 encoding the 67-kDa subunit reveals homology to other ATPases |
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