Nucleotide sequence and deduced amino acid sequence of Escherichia coli adenine phosphoribosyl-transferase and comparison with other analogous enzymes
The Escherichia coli apt gene has been analyzed and its nucleotide (nt) sequence and the deduced amino acid (aa) sequence compared to those of other phosphoribosyltransferases (PRTs). The apt mRNA has a 102-nt leader sequence which may form alternate secondary structures. The RNA transcript may also...
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Veröffentlicht in: | Gene 1986, Vol.43 (3), p.287-293 |
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creator | Hershey, Howard V. Taylor, Milton W. |
description | The
Escherichia coli
apt gene has been analyzed and its nucleotide (nt) sequence and the deduced amino acid (aa) sequence compared to those of other phosphoribosyltransferases (PRTs). The
apt mRNA has a 102-nt leader sequence which may form alternate secondary structures. The RNA transcript may also form several 3' hairpin structures, which, however, do not appear to act as Rho-independent terminators. All PRTs, including
E. coli adenine PRT (APRT), have a strongly conserved 13-aa sequence, as well as other regions of aa sequence or structural similarity.
E. coli APRT is remarkably similar to the mouse enzyme. |
doi_str_mv | 10.1016/0378-1119(86)90218-0 |
format | Article |
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Escherichia coli
apt gene has been analyzed and its nucleotide (nt) sequence and the deduced amino acid (aa) sequence compared to those of other phosphoribosyltransferases (PRTs). The
apt mRNA has a 102-nt leader sequence which may form alternate secondary structures. The RNA transcript may also form several 3' hairpin structures, which, however, do not appear to act as Rho-independent terminators. All PRTs, including
E. coli adenine PRT (APRT), have a strongly conserved 13-aa sequence, as well as other regions of aa sequence or structural similarity.
E. coli APRT is remarkably similar to the mouse enzyme.</description><identifier>ISSN: 0378-1119</identifier><identifier>EISSN: 1879-0038</identifier><identifier>DOI: 10.1016/0378-1119(86)90218-0</identifier><identifier>CODEN: GENED6</identifier><language>eng</language><publisher>Lausanne: Elsevier B.V</publisher><subject>Biological and medical sciences ; conserved sequences ; Escherichia coli ; Fundamental and applied biological sciences. Psychology ; Genes. Genome ; homologies among phosphoribosyltransferases ; Molecular and cellular biology ; Molecular genetics ; purine salvage enzymes ; Recombinant DNA</subject><ispartof>Gene, 1986, Vol.43 (3), p.287-293</ispartof><rights>1986</rights><rights>1987 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c279t-a3031145454be5a02bcaf7084532ea51e7d214c619ac52d2f1fc68f0d79c17a23</citedby><cites>FETCH-LOGICAL-c279t-a3031145454be5a02bcaf7084532ea51e7d214c619ac52d2f1fc68f0d79c17a23</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(86)90218-0$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,781,785,3551,4025,27928,27929,27930,46000</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8120846$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Hershey, Howard V.</creatorcontrib><creatorcontrib>Taylor, Milton W.</creatorcontrib><title>Nucleotide sequence and deduced amino acid sequence of Escherichia coli adenine phosphoribosyl-transferase and comparison with other analogous enzymes</title><title>Gene</title><description>The
Escherichia coli
apt gene has been analyzed and its nucleotide (nt) sequence and the deduced amino acid (aa) sequence compared to those of other phosphoribosyltransferases (PRTs). The
apt mRNA has a 102-nt leader sequence which may form alternate secondary structures. The RNA transcript may also form several 3' hairpin structures, which, however, do not appear to act as Rho-independent terminators. All PRTs, including
E. coli adenine PRT (APRT), have a strongly conserved 13-aa sequence, as well as other regions of aa sequence or structural similarity.
E. coli APRT is remarkably similar to the mouse enzyme.</description><subject>Biological and medical sciences</subject><subject>conserved sequences</subject><subject>Escherichia coli</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes. Genome</subject><subject>homologies among phosphoribosyltransferases</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>purine salvage enzymes</subject><subject>Recombinant DNA</subject><issn>0378-1119</issn><issn>1879-0038</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><recordid>eNp9kc9uFDEMxiMEEsvCG3DIASE4DE0yk_lzQUJVaZGq9gLnyOs4bNDMZIlnqZYH6fOSZatyI1EUKf75i_1ZiNdafdBKt2eq7vpKaz2869v3gzK6r9QTsdJ9N1RK1f1TsXpEnosXzD9UWdaalbi_2eNIaYmeJNPPPc1IEmYvPfk9kpcwxTlJwOj_xVOQF4xbyhG3ESSmMUrwNMeZ5G6buJwcN4kPY7VkmDlQBj7JYpp2kCOnWd7FZSvTUmRKBMb0Pe1Z0vz7MBG_FM8CjEyvHu61-Pb54uv5VXV9e_nl_NN1haYblgpqVWvd2LI3ZEGZDULoVN_Y2hBYTZ03usFWD4DWeBN0wLYPyncD6g5MvRZvT7q7nEpzvLgpMtI4wkylHKebrmmstQVsTiDmxJwpuF2OE-SD08odh-CODrujw65v3d8hlKe1ePOgD4wwhuIGRn7M7bUpxbYF-3jCqPT6K1J2jPFotY-ZcHE-xf__8wflM56N</recordid><startdate>1986</startdate><enddate>1986</enddate><creator>Hershey, Howard V.</creator><creator>Taylor, Milton W.</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope></search><sort><creationdate>1986</creationdate><title>Nucleotide sequence and deduced amino acid sequence of Escherichia coli adenine phosphoribosyl-transferase and comparison with other analogous enzymes</title><author>Hershey, Howard V. ; Taylor, Milton W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c279t-a3031145454be5a02bcaf7084532ea51e7d214c619ac52d2f1fc68f0d79c17a23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>Biological and medical sciences</topic><topic>conserved sequences</topic><topic>Escherichia coli</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes. Genome</topic><topic>homologies among phosphoribosyltransferases</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>purine salvage enzymes</topic><topic>Recombinant DNA</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hershey, Howard V.</creatorcontrib><creatorcontrib>Taylor, Milton W.</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>Gene</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hershey, Howard V.</au><au>Taylor, Milton W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Nucleotide sequence and deduced amino acid sequence of Escherichia coli adenine phosphoribosyl-transferase and comparison with other analogous enzymes</atitle><jtitle>Gene</jtitle><date>1986</date><risdate>1986</risdate><volume>43</volume><issue>3</issue><spage>287</spage><epage>293</epage><pages>287-293</pages><issn>0378-1119</issn><eissn>1879-0038</eissn><coden>GENED6</coden><abstract>The
Escherichia coli
apt gene has been analyzed and its nucleotide (nt) sequence and the deduced amino acid (aa) sequence compared to those of other phosphoribosyltransferases (PRTs). The
apt mRNA has a 102-nt leader sequence which may form alternate secondary structures. The RNA transcript may also form several 3' hairpin structures, which, however, do not appear to act as Rho-independent terminators. All PRTs, including
E. coli adenine PRT (APRT), have a strongly conserved 13-aa sequence, as well as other regions of aa sequence or structural similarity.
E. coli APRT is remarkably similar to the mouse enzyme.</abstract><cop>Lausanne</cop><cop>Amsterdam</cop><cop>New York, NY</cop><pub>Elsevier B.V</pub><doi>10.1016/0378-1119(86)90218-0</doi><tpages>7</tpages></addata></record> |
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ispartof | Gene, 1986, Vol.43 (3), p.287-293 |
issn | 0378-1119 1879-0038 |
language | eng |
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source | Access via ScienceDirect (Elsevier) |
subjects | Biological and medical sciences conserved sequences Escherichia coli Fundamental and applied biological sciences. Psychology Genes. Genome homologies among phosphoribosyltransferases Molecular and cellular biology Molecular genetics purine salvage enzymes Recombinant DNA |
title | Nucleotide sequence and deduced amino acid sequence of Escherichia coli adenine phosphoribosyl-transferase and comparison with other analogous enzymes |
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