Cloning and sequencing of the genes encoding glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase and triosephosphate isomerase ( gap operon) from mesophilic Bacillus megaterium: comparison with corresponding sequences from thermophilic Bacillus stearothermophilus
The structural genes encoding glyceraldehyde-3-phosphate dehydrogenase (GAPDH), 3-phosphoglycerate kinase (PGK) and the N-terminal part of triosephosphate isomerase (TIM) from mesophilic Bacillus megaterium DSM319 have been cloned as a gene cluster ( gap operon) by complementation of an Escherichia...
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| Veröffentlicht in: | Gene 1992-12, Vol.122 (1), p.53-62 |
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| description | The structural genes encoding glyceraldehyde-3-phosphate dehydrogenase (GAPDH), 3-phosphoglycerate kinase (PGK) and the N-terminal part of triosephosphate isomerase (TIM) from mesophilic
Bacillus megaterium DSM319 have been cloned as a gene cluster (
gap operon) by complementation of an
Escherichia coli gap amber mutant. Subsequently, the entire
tpi gene, encoding TIM, was isolated by colony hybridization using a homologous probe. Nucleotide (nt) sequence analysis revealed an unidentified open reading frame (
urf1) of 1029 bp located 50 nt upstream from the start codon of the
gap gene. Gene expression from subclones containing different coding regions was studied by enzyme assay and SDS-PAGE. Both GAPDH and TIM are synthesized in transformed
E. coli cells, whereas PGK is not. There is no unequivocal evidence for
urf1 expression. Two putative promoter sites are present: one 100 nt upstream from
urf1 and one 200 nt upstream from the
pgk gene. An inverted repeat following the second promoter site is postulated to be involved in the transcriptional regulation of the operon. Each coding region shows a G+C content of 40% attained by the adaptation of the G+C content of the third base in the codon to compensate the G+C content of the first and second bases. The deduced amino acid (aa) sequences of
B. megaterium GAPDH, PGK and TIM were compared with those from the thermophilic
Bacillus stearothermophilus by antisymmetrical matrices. The detected characteristic thermophilic-mesophilic exchange pattern concerning aa substitutions between hydrophobic-polar and charged-charged residues corresponds to data obtained for thermophilic and mesophilic lactate dehydrogenases (LDH). The determination of the thermostability of these enzymes revealed two regions of stability for
B. megaterium TIM at high enzyme concentrations. Heat treatment seems to be responsible for the conversion of two differently active conformations or the induction of a new quaternary structure. |
| doi_str_mv | 10.1016/0378-1119(92)90031-J |
| format | Article |
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Bacillus megaterium DSM319 have been cloned as a gene cluster (
gap operon) by complementation of an
Escherichia coli gap amber mutant. Subsequently, the entire
tpi gene, encoding TIM, was isolated by colony hybridization using a homologous probe. Nucleotide (nt) sequence analysis revealed an unidentified open reading frame (
urf1) of 1029 bp located 50 nt upstream from the start codon of the
gap gene. Gene expression from subclones containing different coding regions was studied by enzyme assay and SDS-PAGE. Both GAPDH and TIM are synthesized in transformed
E. coli cells, whereas PGK is not. There is no unequivocal evidence for
urf1 expression. Two putative promoter sites are present: one 100 nt upstream from
urf1 and one 200 nt upstream from the
pgk gene. An inverted repeat following the second promoter site is postulated to be involved in the transcriptional regulation of the operon. Each coding region shows a G+C content of 40% attained by the adaptation of the G+C content of the third base in the codon to compensate the G+C content of the first and second bases. The deduced amino acid (aa) sequences of
B. megaterium GAPDH, PGK and TIM were compared with those from the thermophilic
Bacillus stearothermophilus by antisymmetrical matrices. The detected characteristic thermophilic-mesophilic exchange pattern concerning aa substitutions between hydrophobic-polar and charged-charged residues corresponds to data obtained for thermophilic and mesophilic lactate dehydrogenases (LDH). The determination of the thermostability of these enzymes revealed two regions of stability for
B. megaterium TIM at high enzyme concentrations. Heat treatment seems to be responsible for the conversion of two differently active conformations or the induction of a new quaternary structure.</description><identifier>ISSN: 0378-1119</identifier><identifier>EISSN: 1879-0038</identifier><identifier>DOI: 10.1016/0378-1119(92)90031-J</identifier><identifier>PMID: 1452037</identifier><identifier>CODEN: GENED6</identifier><language>eng</language><publisher>Lausanne: Elsevier B.V</publisher><subject>3-phosphoglycerate kinase ; Amino Acid Sequence ; amino acid sequence exchanges ; Bacillus megaterium ; Bacillus megaterium - enzymology ; Bacillus megaterium - genetics ; Base Sequence ; Biological and medical sciences ; Cloning, Molecular ; DNA, Bacterial ; Electrophoresis, Polyacrylamide Gel ; Enzyme Stability ; Exons ; expression ; Fundamental and applied biological sciences. Psychology ; G+C content ; gap operon ; genes ; Genes. Genome ; Geobacillus stearothermophilus - enzymology ; Geobacillus stearothermophilus - genetics ; glyceraldehyde-3-phosphate dehydrogenase ; Glyceraldehyde-3-Phosphate Dehydrogenases - genetics ; Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism ; Hot Temperature ; Introns ; Molecular and cellular biology ; Molecular genetics ; Molecular Sequence Data ; nucleotide sequence ; Open Reading Frames ; Operon ; operons ; Phosphoglycerate Kinase - genetics ; Phosphoglycerate Kinase - metabolism ; predictions ; Recombinant DNA ; Restriction Mapping ; thermostability ; transcriptional regulation ; Triose-Phosphate Isomerase - genetics ; Triose-Phosphate Isomerase - metabolism ; triosephosphate isomerase</subject><ispartof>Gene, 1992-12, Vol.122 (1), p.53-62</ispartof><rights>1992</rights><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c417t-e036dd287132cdd80eb32a306166a9617f1ac0c7d6fd2293ae2deceaaedb43d43</citedby><cites>FETCH-LOGICAL-c417t-e036dd287132cdd80eb32a306166a9617f1ac0c7d6fd2293ae2deceaaedb43d43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0378-1119(92)90031-J$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3549,27923,27924,45994</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4432357$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1452037$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schläpfer, Beatrice S.</creatorcontrib><creatorcontrib>Zuber, Herbert</creatorcontrib><title>Cloning and sequencing of the genes encoding glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase and triosephosphate isomerase ( gap operon) from mesophilic Bacillus megaterium: comparison with corresponding sequences from thermophilic Bacillus stearothermophilus</title><title>Gene</title><addtitle>Gene</addtitle><description>The structural genes encoding glyceraldehyde-3-phosphate dehydrogenase (GAPDH), 3-phosphoglycerate kinase (PGK) and the N-terminal part of triosephosphate isomerase (TIM) from mesophilic
Bacillus megaterium DSM319 have been cloned as a gene cluster (
gap operon) by complementation of an
Escherichia coli gap amber mutant. Subsequently, the entire
tpi gene, encoding TIM, was isolated by colony hybridization using a homologous probe. Nucleotide (nt) sequence analysis revealed an unidentified open reading frame (
urf1) of 1029 bp located 50 nt upstream from the start codon of the
gap gene. Gene expression from subclones containing different coding regions was studied by enzyme assay and SDS-PAGE. Both GAPDH and TIM are synthesized in transformed
E. coli cells, whereas PGK is not. There is no unequivocal evidence for
urf1 expression. Two putative promoter sites are present: one 100 nt upstream from
urf1 and one 200 nt upstream from the
pgk gene. An inverted repeat following the second promoter site is postulated to be involved in the transcriptional regulation of the operon. Each coding region shows a G+C content of 40% attained by the adaptation of the G+C content of the third base in the codon to compensate the G+C content of the first and second bases. The deduced amino acid (aa) sequences of
B. megaterium GAPDH, PGK and TIM were compared with those from the thermophilic
Bacillus stearothermophilus by antisymmetrical matrices. The detected characteristic thermophilic-mesophilic exchange pattern concerning aa substitutions between hydrophobic-polar and charged-charged residues corresponds to data obtained for thermophilic and mesophilic lactate dehydrogenases (LDH). The determination of the thermostability of these enzymes revealed two regions of stability for
B. megaterium TIM at high enzyme concentrations. Heat treatment seems to be responsible for the conversion of two differently active conformations or the induction of a new quaternary structure.</description><subject>3-phosphoglycerate kinase</subject><subject>Amino Acid Sequence</subject><subject>amino acid sequence exchanges</subject><subject>Bacillus megaterium</subject><subject>Bacillus megaterium - enzymology</subject><subject>Bacillus megaterium - genetics</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Cloning, Molecular</subject><subject>DNA, Bacterial</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzyme Stability</subject><subject>Exons</subject><subject>expression</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>G+C content</subject><subject>gap operon</subject><subject>genes</subject><subject>Genes. Genome</subject><subject>Geobacillus stearothermophilus - enzymology</subject><subject>Geobacillus stearothermophilus - genetics</subject><subject>glyceraldehyde-3-phosphate dehydrogenase</subject><subject>Glyceraldehyde-3-Phosphate Dehydrogenases - genetics</subject><subject>Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism</subject><subject>Hot Temperature</subject><subject>Introns</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>nucleotide sequence</subject><subject>Open Reading Frames</subject><subject>Operon</subject><subject>operons</subject><subject>Phosphoglycerate Kinase - genetics</subject><subject>Phosphoglycerate Kinase - metabolism</subject><subject>predictions</subject><subject>Recombinant DNA</subject><subject>Restriction Mapping</subject><subject>thermostability</subject><subject>transcriptional regulation</subject><subject>Triose-Phosphate Isomerase - genetics</subject><subject>Triose-Phosphate Isomerase - metabolism</subject><subject>triosephosphate isomerase</subject><issn>0378-1119</issn><issn>1879-0038</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUkuLFDEQbkVZx9WjN4UcRHbB1rymHx4EHXwtC170HDJJ9XS0u9Ob6lbm35t-sHMQNJdQ9T1SFb4kecroK0ZZ9pqKvEgZY-VFyS9LSgVLr-4mG1bkZRqr4l6yuaU8SB4i_qDxbLf8LDljcssjuLnzZNf4znUHojtLEG5G6MxU-ooMNZADdIAk9ryduofmaCDoxkJ9tJCKtK899rUegMyt4KNAI7wkC-BXQcR_ugmYnxmC8wgnqUPfRlJEL8hB98T3EHx3SargW9IC-r52jTPkvTauaUaMvUPUBTe2b4jxba9DtOjIbzfUsQ4BsPfdPPC6UdxhNosrhfYvOxxAB3_CRnyU3K90g_B4vc-T7x8_fNt9Tq-_fvqye3edGsnyIQUqMmt5kTPBjbUFhb3gWtCMZZkuM5ZXTBtqcptVlvNSaOAWDGgNdi-FleI8ebH49sHHQXFQrUMDTaM78COqXEjKuaT_JbJMZlTmeSTKhWiCRwxQqT64VoejYlRNsVFTJtSUCVVyNcdGXUXZs9V_3LdgT6IlJxF_vuIajW6qoGNM8JYmpeBiO9HeLjSIn_bLQVBo3PT_1gUwg7Le_XuOP4lH6Gc</recordid><startdate>19921201</startdate><enddate>19921201</enddate><creator>Schläpfer, Beatrice S.</creator><creator>Zuber, Herbert</creator><general>Elsevier B.V</general><general>Elsevier</general><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>19921201</creationdate><title>Cloning and sequencing of the genes encoding glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase and triosephosphate isomerase ( gap operon) from mesophilic Bacillus megaterium: comparison with corresponding sequences from thermophilic Bacillus stearothermophilus</title><author>Schläpfer, Beatrice S. ; Zuber, Herbert</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c417t-e036dd287132cdd80eb32a306166a9617f1ac0c7d6fd2293ae2deceaaedb43d43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>3-phosphoglycerate kinase</topic><topic>Amino Acid Sequence</topic><topic>amino acid sequence exchanges</topic><topic>Bacillus megaterium</topic><topic>Bacillus megaterium - enzymology</topic><topic>Bacillus megaterium - genetics</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Cloning, Molecular</topic><topic>DNA, Bacterial</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzyme Stability</topic><topic>Exons</topic><topic>expression</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>G+C content</topic><topic>gap operon</topic><topic>genes</topic><topic>Genes. Genome</topic><topic>Geobacillus stearothermophilus - enzymology</topic><topic>Geobacillus stearothermophilus - genetics</topic><topic>glyceraldehyde-3-phosphate dehydrogenase</topic><topic>Glyceraldehyde-3-Phosphate Dehydrogenases - genetics</topic><topic>Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism</topic><topic>Hot Temperature</topic><topic>Introns</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>nucleotide sequence</topic><topic>Open Reading Frames</topic><topic>Operon</topic><topic>operons</topic><topic>Phosphoglycerate Kinase - genetics</topic><topic>Phosphoglycerate Kinase - metabolism</topic><topic>predictions</topic><topic>Recombinant DNA</topic><topic>Restriction Mapping</topic><topic>thermostability</topic><topic>transcriptional regulation</topic><topic>Triose-Phosphate Isomerase - genetics</topic><topic>Triose-Phosphate Isomerase - metabolism</topic><topic>triosephosphate isomerase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schläpfer, Beatrice S.</creatorcontrib><creatorcontrib>Zuber, Herbert</creatorcontrib><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>Gene</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schläpfer, Beatrice S.</au><au>Zuber, Herbert</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning and sequencing of the genes encoding glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase and triosephosphate isomerase ( gap operon) from mesophilic Bacillus megaterium: comparison with corresponding sequences from thermophilic Bacillus stearothermophilus</atitle><jtitle>Gene</jtitle><addtitle>Gene</addtitle><date>1992-12-01</date><risdate>1992</risdate><volume>122</volume><issue>1</issue><spage>53</spage><epage>62</epage><pages>53-62</pages><issn>0378-1119</issn><eissn>1879-0038</eissn><coden>GENED6</coden><abstract>The structural genes encoding glyceraldehyde-3-phosphate dehydrogenase (GAPDH), 3-phosphoglycerate kinase (PGK) and the N-terminal part of triosephosphate isomerase (TIM) from mesophilic
Bacillus megaterium DSM319 have been cloned as a gene cluster (
gap operon) by complementation of an
Escherichia coli gap amber mutant. Subsequently, the entire
tpi gene, encoding TIM, was isolated by colony hybridization using a homologous probe. Nucleotide (nt) sequence analysis revealed an unidentified open reading frame (
urf1) of 1029 bp located 50 nt upstream from the start codon of the
gap gene. Gene expression from subclones containing different coding regions was studied by enzyme assay and SDS-PAGE. Both GAPDH and TIM are synthesized in transformed
E. coli cells, whereas PGK is not. There is no unequivocal evidence for
urf1 expression. Two putative promoter sites are present: one 100 nt upstream from
urf1 and one 200 nt upstream from the
pgk gene. An inverted repeat following the second promoter site is postulated to be involved in the transcriptional regulation of the operon. Each coding region shows a G+C content of 40% attained by the adaptation of the G+C content of the third base in the codon to compensate the G+C content of the first and second bases. The deduced amino acid (aa) sequences of
B. megaterium GAPDH, PGK and TIM were compared with those from the thermophilic
Bacillus stearothermophilus by antisymmetrical matrices. The detected characteristic thermophilic-mesophilic exchange pattern concerning aa substitutions between hydrophobic-polar and charged-charged residues corresponds to data obtained for thermophilic and mesophilic lactate dehydrogenases (LDH). The determination of the thermostability of these enzymes revealed two regions of stability for
B. megaterium TIM at high enzyme concentrations. Heat treatment seems to be responsible for the conversion of two differently active conformations or the induction of a new quaternary structure.</abstract><cop>Lausanne</cop><cop>Amsterdam</cop><cop>New York, NY</cop><pub>Elsevier B.V</pub><pmid>1452037</pmid><doi>10.1016/0378-1119(92)90031-J</doi><tpages>10</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0378-1119 |
| ispartof | Gene, 1992-12, Vol.122 (1), p.53-62 |
| issn | 0378-1119 1879-0038 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_73402240 |
| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | 3-phosphoglycerate kinase Amino Acid Sequence amino acid sequence exchanges Bacillus megaterium Bacillus megaterium - enzymology Bacillus megaterium - genetics Base Sequence Biological and medical sciences Cloning, Molecular DNA, Bacterial Electrophoresis, Polyacrylamide Gel Enzyme Stability Exons expression Fundamental and applied biological sciences. Psychology G+C content gap operon genes Genes. Genome Geobacillus stearothermophilus - enzymology Geobacillus stearothermophilus - genetics glyceraldehyde-3-phosphate dehydrogenase Glyceraldehyde-3-Phosphate Dehydrogenases - genetics Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism Hot Temperature Introns Molecular and cellular biology Molecular genetics Molecular Sequence Data nucleotide sequence Open Reading Frames Operon operons Phosphoglycerate Kinase - genetics Phosphoglycerate Kinase - metabolism predictions Recombinant DNA Restriction Mapping thermostability transcriptional regulation Triose-Phosphate Isomerase - genetics Triose-Phosphate Isomerase - metabolism triosephosphate isomerase |
| title | Cloning and sequencing of the genes encoding glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase and triosephosphate isomerase ( gap operon) from mesophilic Bacillus megaterium: comparison with corresponding sequences from thermophilic Bacillus stearothermophilus |
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