Analysis of the nucleotide and derived amino acid sequences of the SsoII restriction endonuclease and methyltransferase
A 2648-bp fragment from the P4 plasmid of Shigella sonnei strain 47 coding for the Ssoll restriction endonuclease (ENase) and methyltransferase (MTase) (recognition sequence 5'-CCNGG) was sequenced. Two divergently arranged open reading frames of 905 bp for the Ssoll ENase (R· Ssoll) and 1137 b...
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| Veröffentlicht in: | Gene 1993-02, Vol.124 (1), p.13-19 |
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| creator | Karyagina, Anna S. Lunin, Vladimir G. Degtyarenko, Kirill N. Uvarovc, Valentin Y. Nikolskaya, Irina I. |
| description | A 2648-bp fragment from the P4 plasmid of
Shigella sonnei strain 47 coding for the
Ssoll restriction endonuclease (ENase) and methyltransferase (MTase) (recognition sequence 5'-CCNGG) was sequenced. Two divergently arranged open reading frames of 905 bp for the Ssoll ENase (R·
Ssoll) and 1137 bp for the MTase (M ·
SsoII) were identified. The coding regions are separated by 110 bp. The calculated
M
r of R·
SsoII (35937) and M·
SsoII (42887) are in good agreement with values previously obtained by in vitro transcription-translation experiments i.e., 35 and 43 kDa for the ENase and MTase, respectively. The M ·
SsoII amino acid (aa) sequence revealed a considerable similarity to m
5C-MTases recognizing the related sequences — M·
EcoRII, M·dem, M·
MspI, M·
BsuFI, M-
HpaII, and M·
HhaI. Surprisingly, the greatest degree of homology has been observed between the aa sequences of M ·
SsoII and M·
NlaX, with an unidentified recognition sequence. The multiple alignment of aa sequences helps to identify the blocks of conserved aa in variable regions of MTases. These conserved aa can play a key role in target recognition. Some aspects of evolution of m
5C-MTases are discussed. |
| doi_str_mv | 10.1016/0378-1119(93)90756-S |
| format | Article |
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Shigella sonnei strain 47 coding for the
Ssoll restriction endonuclease (ENase) and methyltransferase (MTase) (recognition sequence 5'-CCNGG) was sequenced. Two divergently arranged open reading frames of 905 bp for the Ssoll ENase (R·
Ssoll) and 1137 bp for the MTase (M ·
SsoII) were identified. The coding regions are separated by 110 bp. The calculated
M
r of R·
SsoII (35937) and M·
SsoII (42887) are in good agreement with values previously obtained by in vitro transcription-translation experiments i.e., 35 and 43 kDa for the ENase and MTase, respectively. The M ·
SsoII amino acid (aa) sequence revealed a considerable similarity to m
5C-MTases recognizing the related sequences — M·
EcoRII, M·dem, M·
MspI, M·
BsuFI, M-
HpaII, and M·
HhaI. Surprisingly, the greatest degree of homology has been observed between the aa sequences of M ·
SsoII and M·
NlaX, with an unidentified recognition sequence. The multiple alignment of aa sequences helps to identify the blocks of conserved aa in variable regions of MTases. These conserved aa can play a key role in target recognition. Some aspects of evolution of m
5C-MTases are discussed.</description><identifier>ISSN: 0378-1119</identifier><identifier>EISSN: 1879-0038</identifier><identifier>DOI: 10.1016/0378-1119(93)90756-S</identifier><identifier>PMID: 7916706</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Amino Acid Sequence ; amino acid sequence similarities ; Base Sequence ; Codon - genetics ; deoxyribonuclease SsoII ; Deoxyribonucleases, Type II Site-Specific - genetics ; Deoxyribonucleases, Type II Site-Specific - metabolism ; DNA methyltransferase SsoII ; DNA Restriction Enzymes - genetics ; DNA, Bacterial - genetics ; DNA-Cytosine Methylases - genetics ; Escherichia coli ; Escherichia coli - enzymology ; Escherichia coli - genetics ; Gene Expression Regulation, Bacterial ; Gene Expression Regulation, Enzymologic ; genes ; Genes, Bacterial ; m 5C-methyltransferase ; Molecular Sequence Data ; nucleotide sequence ; Phylogeny ; Plasmids ; predictions ; restriction-modification ; restriction-modification system ; Sequence Homology, Amino Acid ; Shigella sonnei ; Shigella sonnei - enzymology ; Shigella sonnei - genetics ; Substrate Specificity ; Transcription, Genetic</subject><ispartof>Gene, 1993-02, Vol.124 (1), p.13-19</ispartof><rights>1993</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c388t-ded97e03ee8f3585bb4a6afcc4b1eb6bd8fd71aef40a406d90591218ce45a1b43</citedby><cites>FETCH-LOGICAL-c388t-ded97e03ee8f3585bb4a6afcc4b1eb6bd8fd71aef40a406d90591218ce45a1b43</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(93)90756-S$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7916706$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Karyagina, Anna S.</creatorcontrib><creatorcontrib>Lunin, Vladimir G.</creatorcontrib><creatorcontrib>Degtyarenko, Kirill N.</creatorcontrib><creatorcontrib>Uvarovc, Valentin Y.</creatorcontrib><creatorcontrib>Nikolskaya, Irina I.</creatorcontrib><title>Analysis of the nucleotide and derived amino acid sequences of the SsoII restriction endonuclease and methyltransferase</title><title>Gene</title><addtitle>Gene</addtitle><description>A 2648-bp fragment from the P4 plasmid of
Shigella sonnei strain 47 coding for the
Ssoll restriction endonuclease (ENase) and methyltransferase (MTase) (recognition sequence 5'-CCNGG) was sequenced. Two divergently arranged open reading frames of 905 bp for the Ssoll ENase (R·
Ssoll) and 1137 bp for the MTase (M ·
SsoII) were identified. The coding regions are separated by 110 bp. The calculated
M
r of R·
SsoII (35937) and M·
SsoII (42887) are in good agreement with values previously obtained by in vitro transcription-translation experiments i.e., 35 and 43 kDa for the ENase and MTase, respectively. The M ·
SsoII amino acid (aa) sequence revealed a considerable similarity to m
5C-MTases recognizing the related sequences — M·
EcoRII, M·dem, M·
MspI, M·
BsuFI, M-
HpaII, and M·
HhaI. Surprisingly, the greatest degree of homology has been observed between the aa sequences of M ·
SsoII and M·
NlaX, with an unidentified recognition sequence. The multiple alignment of aa sequences helps to identify the blocks of conserved aa in variable regions of MTases. These conserved aa can play a key role in target recognition. Some aspects of evolution of m
5C-MTases are discussed.</description><subject>Amino Acid Sequence</subject><subject>amino acid sequence similarities</subject><subject>Base Sequence</subject><subject>Codon - genetics</subject><subject>deoxyribonuclease SsoII</subject><subject>Deoxyribonucleases, Type II Site-Specific - genetics</subject><subject>Deoxyribonucleases, Type II Site-Specific - metabolism</subject><subject>DNA methyltransferase SsoII</subject><subject>DNA Restriction Enzymes - genetics</subject><subject>DNA, Bacterial - genetics</subject><subject>DNA-Cytosine Methylases - genetics</subject><subject>Escherichia coli</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - genetics</subject><subject>Gene Expression Regulation, Bacterial</subject><subject>Gene Expression Regulation, Enzymologic</subject><subject>genes</subject><subject>Genes, Bacterial</subject><subject>m 5C-methyltransferase</subject><subject>Molecular Sequence Data</subject><subject>nucleotide sequence</subject><subject>Phylogeny</subject><subject>Plasmids</subject><subject>predictions</subject><subject>restriction-modification</subject><subject>restriction-modification system</subject><subject>Sequence Homology, Amino Acid</subject><subject>Shigella sonnei</subject><subject>Shigella sonnei - enzymology</subject><subject>Shigella sonnei - genetics</subject><subject>Substrate Specificity</subject><subject>Transcription, Genetic</subject><issn>0378-1119</issn><issn>1879-0038</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1OAyEUhYnRaK2-gSasjC5GocwwsDExxp8mTVxU14SBOxEzAwq0pm_v1DZdKhsS7jnnku8gdEbJNSWU3xBWi4JSKi8lu5Kkrngx30MjKmpZEMLEPhrtJEfoOKUPMpyqmhyiw1pSXhM-Qt93Xner5BIOLc7vgP3CdBCys4C1t9hCdEuwWPfOB6yNszjB1wK8gZ1lnsJ0iiOkHJ3JLngM3obfIJ02MT3k91WXo_aphTi8nqCDVncJTrf3GL09PrzePxezl6fp_d2sMEyIXFiwsgbCAETLKlE1Tam5bo0pGwoNb6xobU01tCXRJeFWkkrSCRUGykrTpmRjdLHJ_Yxh-HbKqnfJQNdpD2GR1ECNVnLC_xVSXk54zdggLDdCE0NKEVr1GV2v40pRotbFqDV1taauJFO_xaj5YDvf5i-aHuzOtG1imN9u5jDQWDqIKhm3xmxdBJOVDe7vBT8JN6AJ</recordid><startdate>19930214</startdate><enddate>19930214</enddate><creator>Karyagina, Anna S.</creator><creator>Lunin, Vladimir G.</creator><creator>Degtyarenko, Kirill N.</creator><creator>Uvarovc, Valentin Y.</creator><creator>Nikolskaya, Irina I.</creator><general>Elsevier B.V</general><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>19930214</creationdate><title>Analysis of the nucleotide and derived amino acid sequences of the SsoII restriction endonuclease and methyltransferase</title><author>Karyagina, Anna S. ; Lunin, Vladimir G. ; Degtyarenko, Kirill N. ; Uvarovc, Valentin Y. ; Nikolskaya, Irina I.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c388t-ded97e03ee8f3585bb4a6afcc4b1eb6bd8fd71aef40a406d90591218ce45a1b43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Amino Acid Sequence</topic><topic>amino acid sequence similarities</topic><topic>Base Sequence</topic><topic>Codon - genetics</topic><topic>deoxyribonuclease SsoII</topic><topic>Deoxyribonucleases, Type II Site-Specific - genetics</topic><topic>Deoxyribonucleases, Type II Site-Specific - metabolism</topic><topic>DNA methyltransferase SsoII</topic><topic>DNA Restriction Enzymes - genetics</topic><topic>DNA, Bacterial - genetics</topic><topic>DNA-Cytosine Methylases - genetics</topic><topic>Escherichia coli</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - genetics</topic><topic>Gene Expression Regulation, Bacterial</topic><topic>Gene Expression Regulation, Enzymologic</topic><topic>genes</topic><topic>Genes, Bacterial</topic><topic>m 5C-methyltransferase</topic><topic>Molecular Sequence Data</topic><topic>nucleotide sequence</topic><topic>Phylogeny</topic><topic>Plasmids</topic><topic>predictions</topic><topic>restriction-modification</topic><topic>restriction-modification system</topic><topic>Sequence Homology, Amino Acid</topic><topic>Shigella sonnei</topic><topic>Shigella sonnei - enzymology</topic><topic>Shigella sonnei - genetics</topic><topic>Substrate Specificity</topic><topic>Transcription, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Karyagina, Anna S.</creatorcontrib><creatorcontrib>Lunin, Vladimir G.</creatorcontrib><creatorcontrib>Degtyarenko, Kirill N.</creatorcontrib><creatorcontrib>Uvarovc, Valentin Y.</creatorcontrib><creatorcontrib>Nikolskaya, Irina I.</creatorcontrib><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>Karyagina, Anna S.</au><au>Lunin, Vladimir G.</au><au>Degtyarenko, Kirill N.</au><au>Uvarovc, Valentin Y.</au><au>Nikolskaya, Irina I.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Analysis of the nucleotide and derived amino acid sequences of the SsoII restriction endonuclease and methyltransferase</atitle><jtitle>Gene</jtitle><addtitle>Gene</addtitle><date>1993-02-14</date><risdate>1993</risdate><volume>124</volume><issue>1</issue><spage>13</spage><epage>19</epage><pages>13-19</pages><issn>0378-1119</issn><eissn>1879-0038</eissn><abstract>A 2648-bp fragment from the P4 plasmid of
Shigella sonnei strain 47 coding for the
Ssoll restriction endonuclease (ENase) and methyltransferase (MTase) (recognition sequence 5'-CCNGG) was sequenced. Two divergently arranged open reading frames of 905 bp for the Ssoll ENase (R·
Ssoll) and 1137 bp for the MTase (M ·
SsoII) were identified. The coding regions are separated by 110 bp. The calculated
M
r of R·
SsoII (35937) and M·
SsoII (42887) are in good agreement with values previously obtained by in vitro transcription-translation experiments i.e., 35 and 43 kDa for the ENase and MTase, respectively. The M ·
SsoII amino acid (aa) sequence revealed a considerable similarity to m
5C-MTases recognizing the related sequences — M·
EcoRII, M·dem, M·
MspI, M·
BsuFI, M-
HpaII, and M·
HhaI. Surprisingly, the greatest degree of homology has been observed between the aa sequences of M ·
SsoII and M·
NlaX, with an unidentified recognition sequence. The multiple alignment of aa sequences helps to identify the blocks of conserved aa in variable regions of MTases. These conserved aa can play a key role in target recognition. Some aspects of evolution of m
5C-MTases are discussed.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>7916706</pmid><doi>10.1016/0378-1119(93)90756-S</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0378-1119 |
| ispartof | Gene, 1993-02, Vol.124 (1), p.13-19 |
| issn | 0378-1119 1879-0038 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_75615926 |
| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Amino Acid Sequence amino acid sequence similarities Base Sequence Codon - genetics deoxyribonuclease SsoII Deoxyribonucleases, Type II Site-Specific - genetics Deoxyribonucleases, Type II Site-Specific - metabolism DNA methyltransferase SsoII DNA Restriction Enzymes - genetics DNA, Bacterial - genetics DNA-Cytosine Methylases - genetics Escherichia coli Escherichia coli - enzymology Escherichia coli - genetics Gene Expression Regulation, Bacterial Gene Expression Regulation, Enzymologic genes Genes, Bacterial m 5C-methyltransferase Molecular Sequence Data nucleotide sequence Phylogeny Plasmids predictions restriction-modification restriction-modification system Sequence Homology, Amino Acid Shigella sonnei Shigella sonnei - enzymology Shigella sonnei - genetics Substrate Specificity Transcription, Genetic |
| title | Analysis of the nucleotide and derived amino acid sequences of the SsoII restriction endonuclease and methyltransferase |
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