Bacillus subtilis alkaline phosphatases III and IV. Cloning, sequencing, and comparisons of deduced amino acid sequence with Escherichia coli alkaline phosphatase three-dimensional structure
Bacillus subtilis has an alkaline phosphatase multigene family. Two members of this gene family, phoAIII and phoAIV, were cloned, taking advantage of in vitro constructed strains containing a plasmid insertion within one or the other of the structural genes. The DNA sequences of the two genes showed...
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| Veröffentlicht in: | The Journal of biological chemistry 1991-01, Vol.266 (2), p.1077-1084 |
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| creator | Hulett, F M Kim, E E Bookstein, C Kapp, N V Edwards, C W Wyckoff, H W |
| description | Bacillus subtilis has an alkaline phosphatase multigene family. Two members of this gene family, phoAIII and phoAIV, were cloned, taking advantage of in vitro constructed strains containing a plasmid insertion within one or the other of the structural genes. The DNA sequences of the two genes showed approximately 64% identity at the DNA level and 63% identity in the deduced primary amino acid sequences. The phoAIII and phoAIV genes code for predicted proteins of 47,149 and 45,935 Da, respectively. Comparison of the deduced primary amino acid sequence of the mature proteins with other sequenced alkaline phosphatases from Escherichia coli, yeast, and humans shows 25-30% identity. Based on the refined crystal structure of E. coli alkaline phosphatase, it appears that the active site and the core of the structure are retained in both Bacillus alkaline phosphatases. However, both proteins are truncated at the amino terminus compared with other mature alkaline phosphatases, three sizable surface loops of E. coli are deleted, and a minidomain is replaced with a larger domain in the model. Neither Bacillus alkaline phosphatase sequenced contains any cysteine residues, an amino acid implicated in intrachain disulfide bond formation in other alkaline phosphatases. |
| doi_str_mv | 10.1016/S0021-9258(17)35285-7 |
| format | Article |
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Cloning, sequencing, and comparisons of deduced amino acid sequence with Escherichia coli alkaline phosphatase three-dimensional structure</title><source>MEDLINE</source><source>Alma/SFX Local Collection</source><source>EZB Electronic Journals Library</source><creator>Hulett, F M ; Kim, E E ; Bookstein, C ; Kapp, N V ; Edwards, C W ; Wyckoff, H W</creator><creatorcontrib>Hulett, F M ; Kim, E E ; Bookstein, C ; Kapp, N V ; Edwards, C W ; Wyckoff, H W</creatorcontrib><description>Bacillus subtilis has an alkaline phosphatase multigene family. Two members of this gene family, phoAIII and phoAIV, were cloned, taking advantage of in vitro constructed strains containing a plasmid insertion within one or the other of the structural genes. The DNA sequences of the two genes showed approximately 64% identity at the DNA level and 63% identity in the deduced primary amino acid sequences. The phoAIII and phoAIV genes code for predicted proteins of 47,149 and 45,935 Da, respectively. Comparison of the deduced primary amino acid sequence of the mature proteins with other sequenced alkaline phosphatases from Escherichia coli, yeast, and humans shows 25-30% identity. Based on the refined crystal structure of E. coli alkaline phosphatase, it appears that the active site and the core of the structure are retained in both Bacillus alkaline phosphatases. However, both proteins are truncated at the amino terminus compared with other mature alkaline phosphatases, three sizable surface loops of E. coli are deleted, and a minidomain is replaced with a larger domain in the model. Neither Bacillus alkaline phosphatase sequenced contains any cysteine residues, an amino acid implicated in intrachain disulfide bond formation in other alkaline phosphatases.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(17)35285-7</identifier><identifier>PMID: 1898729</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Alkaline Phosphatase - genetics ; Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Bacillus subtilis ; Bacillus subtilis - enzymology ; Base Sequence ; Binding Sites ; Biological and medical sciences ; Cloning, Molecular ; DNA, Bacterial - genetics ; Enzymes and enzyme inhibitors ; Escherichia coli - enzymology ; Fundamental and applied biological sciences. 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Cloning, sequencing, and comparisons of deduced amino acid sequence with Escherichia coli alkaline phosphatase three-dimensional structure</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Bacillus subtilis has an alkaline phosphatase multigene family. Two members of this gene family, phoAIII and phoAIV, were cloned, taking advantage of in vitro constructed strains containing a plasmid insertion within one or the other of the structural genes. The DNA sequences of the two genes showed approximately 64% identity at the DNA level and 63% identity in the deduced primary amino acid sequences. The phoAIII and phoAIV genes code for predicted proteins of 47,149 and 45,935 Da, respectively. Comparison of the deduced primary amino acid sequence of the mature proteins with other sequenced alkaline phosphatases from Escherichia coli, yeast, and humans shows 25-30% identity. Based on the refined crystal structure of E. coli alkaline phosphatase, it appears that the active site and the core of the structure are retained in both Bacillus alkaline phosphatases. However, both proteins are truncated at the amino terminus compared with other mature alkaline phosphatases, three sizable surface loops of E. coli are deleted, and a minidomain is replaced with a larger domain in the model. Neither Bacillus alkaline phosphatase sequenced contains any cysteine residues, an amino acid implicated in intrachain disulfide bond formation in other alkaline phosphatases.</description><subject>Alkaline Phosphatase - genetics</subject><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Bacillus subtilis</subject><subject>Bacillus subtilis - enzymology</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Cloning, Molecular</subject><subject>DNA, Bacterial - genetics</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Escherichia coli - enzymology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>genes</subject><subject>Hydrolases</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Plasmids</subject><subject>Protein Conformation</subject><subject>Restriction Mapping</subject><subject>Sequence Homology, Nucleic Acid</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkV2L1DAUhoso67j6ExaCoCjYNR9tml6JDqsOLHjhB96FTHK6jabNmNO6-Of8baYzo3sjbG4SOM_Je5KnKM4YPWeUyZcfKeWsbHmtnrHmuai5qsvmTrFiVIlS1Ozr3WL1D7lfPED8RvOqWnZSnDDVqoa3q-L3G2N9CDMSnLeTDx6JCd9N8COQXR9x15vJICDZbDbEjI5svpyTdYijH69eEIQfM4x2f16KNg47kzzGEUnsiAM3W3DEDH6MJAe5vx1Arv3Ukwu0PSRve29yb_D_zSZTnwBK5wcY0cfRBIJTmu00J3hY3OtMQHh03E-Lz28vPq3fl5cf3m3Wry9LWzHalIKbLQBwa2jFaQ22MUZWru1qwZlQnDFjpW1dZYVQrmtp1_CKUidlzSSoRpwWTw_37lLMD8BJDx4thGBGiDNqRYVsORe3gkzSqhEtzWB9AG2KiAk6vUt-MOmXZlQvgvVesF7sadbovWC9THJ2DJi3A7ibroPRXH9yrBu0JnTJZD94g7WybVSlMvf4wPX-qr_2CfTWx2xj0FxKzfMIzRL26gBB_tufHpJG6xd9LjfYSbvobxn3D1xl0Uo</recordid><startdate>19910115</startdate><enddate>19910115</enddate><creator>Hulett, F M</creator><creator>Kim, E E</creator><creator>Bookstein, C</creator><creator>Kapp, N V</creator><creator>Edwards, C W</creator><creator>Wyckoff, H W</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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>M81</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19910115</creationdate><title>Bacillus subtilis alkaline phosphatases III and IV. Cloning, sequencing, and comparisons of deduced amino acid sequence with Escherichia coli alkaline phosphatase three-dimensional structure</title><author>Hulett, F M ; Kim, E E ; Bookstein, C ; Kapp, N V ; Edwards, C W ; Wyckoff, H W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4107-32abeee2ca04205ec7aa64d9f532138211ac6c9d4c338df90f72400d66516e873</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Alkaline Phosphatase - genetics</topic><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Bacillus subtilis</topic><topic>Bacillus subtilis - enzymology</topic><topic>Base Sequence</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Cloning, Molecular</topic><topic>DNA, Bacterial - genetics</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Escherichia coli - enzymology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>genes</topic><topic>Hydrolases</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>Plasmids</topic><topic>Protein Conformation</topic><topic>Restriction Mapping</topic><topic>Sequence Homology, Nucleic Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hulett, F M</creatorcontrib><creatorcontrib>Kim, E E</creatorcontrib><creatorcontrib>Bookstein, C</creatorcontrib><creatorcontrib>Kapp, N V</creatorcontrib><creatorcontrib>Edwards, C W</creatorcontrib><creatorcontrib>Wyckoff, H W</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>Biochemistry Abstracts 3</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>Hulett, F M</au><au>Kim, E E</au><au>Bookstein, C</au><au>Kapp, N V</au><au>Edwards, C W</au><au>Wyckoff, H W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Bacillus subtilis alkaline phosphatases III and IV. Cloning, sequencing, and comparisons of deduced amino acid sequence with Escherichia coli alkaline phosphatase three-dimensional structure</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1991-01-15</date><risdate>1991</risdate><volume>266</volume><issue>2</issue><spage>1077</spage><epage>1084</epage><pages>1077-1084</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Bacillus subtilis has an alkaline phosphatase multigene family. Two members of this gene family, phoAIII and phoAIV, were cloned, taking advantage of in vitro constructed strains containing a plasmid insertion within one or the other of the structural genes. The DNA sequences of the two genes showed approximately 64% identity at the DNA level and 63% identity in the deduced primary amino acid sequences. The phoAIII and phoAIV genes code for predicted proteins of 47,149 and 45,935 Da, respectively. Comparison of the deduced primary amino acid sequence of the mature proteins with other sequenced alkaline phosphatases from Escherichia coli, yeast, and humans shows 25-30% identity. Based on the refined crystal structure of E. coli alkaline phosphatase, it appears that the active site and the core of the structure are retained in both Bacillus alkaline phosphatases. However, both proteins are truncated at the amino terminus compared with other mature alkaline phosphatases, three sizable surface loops of E. coli are deleted, and a minidomain is replaced with a larger domain in the model. Neither Bacillus alkaline phosphatase sequenced contains any cysteine residues, an amino acid implicated in intrachain disulfide bond formation in other alkaline phosphatases.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>1898729</pmid><doi>10.1016/S0021-9258(17)35285-7</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1991-01, Vol.266 (2), p.1077-1084 |
| issn | 0021-9258 1083-351X |
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| source | MEDLINE; Alma/SFX Local Collection; EZB Electronic Journals Library |
| subjects | Alkaline Phosphatase - genetics Amino Acid Sequence Analytical, structural and metabolic biochemistry Bacillus subtilis Bacillus subtilis - enzymology Base Sequence Binding Sites Biological and medical sciences Cloning, Molecular DNA, Bacterial - genetics Enzymes and enzyme inhibitors Escherichia coli - enzymology Fundamental and applied biological sciences. Psychology genes Hydrolases Molecular Sequence Data Mutation Plasmids Protein Conformation Restriction Mapping Sequence Homology, Nucleic Acid |
| title | Bacillus subtilis alkaline phosphatases III and IV. Cloning, sequencing, and comparisons of deduced amino acid sequence with Escherichia coli alkaline phosphatase three-dimensional structure |
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