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Regulation of Polyamine Biosynthesis in Escherichia coli by Basic Proteins
In Escherichia coli, the biosynthetic ornithine and arginine decarboxylases (EC 4.1.1.17 and 4.1.1.19, respectively) are responsible for the biosynthesis of polyamines from ornithine and arginine, respectively. When E. coli cells are grown in the presence of increasing amounts of polyamines, a progr...
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Published in: | Proceedings of the National Academy of Sciences - PNAS 1983-09, Vol.80 (17), p.5181-5184 |
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creator | Heller, John S. Rostomily, Robert Kyriakidis, Dimitri A. Canellakis, Evangelos S. |
description | In Escherichia coli, the biosynthetic ornithine and arginine decarboxylases (EC 4.1.1.17 and 4.1.1.19, respectively) are responsible for the biosynthesis of polyamines from ornithine and arginine, respectively. When E. coli cells are grown in the presence of increasing amounts of polyamines, a progressive increase in the amount of antizyme 1 and antizyme 2 occurs. The amino acid compositions of antizymes 1 and 2 show them to be basic proteins; antizyme 1 has an amino acid composition similar to that of the E. coli histone-like protein HU and of the eukaryotic histone H2B; antizyme 2 is characterized by an unusually high arginine content. We find these proteins to be specific inhibitors of both the biosynthetic ornithine decarboxylase and the biosynthetic arginine decarboxylase. They do not inhibit the corresponding biodegradative ornithine and arginine decarboxylases, nor do they inhibit lysine decarboxylase or S-adenosylmethionine decarboxylase. These properties of the antizymes favor their function in the regulation of polyamine biosynthesis in E. coli. The ability of the purified antizymes to inhibit the ornithine and arginine decarboxylases is stabilized in acidic buffers and is lost upon prolonged exposure to solutions at neutral or basic pH. |
doi_str_mv | 10.1073/pnas.80.17.5181 |
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When E. coli cells are grown in the presence of increasing amounts of polyamines, a progressive increase in the amount of antizyme 1 and antizyme 2 occurs. The amino acid compositions of antizymes 1 and 2 show them to be basic proteins; antizyme 1 has an amino acid composition similar to that of the E. coli histone-like protein HU and of the eukaryotic histone H2B; antizyme 2 is characterized by an unusually high arginine content. We find these proteins to be specific inhibitors of both the biosynthetic ornithine decarboxylase and the biosynthetic arginine decarboxylase. They do not inhibit the corresponding biodegradative ornithine and arginine decarboxylases, nor do they inhibit lysine decarboxylase or S-adenosylmethionine decarboxylase. These properties of the antizymes favor their function in the regulation of polyamine biosynthesis in E. coli. The ability of the purified antizymes to inhibit the ornithine and arginine decarboxylases is stabilized in acidic buffers and is lost upon prolonged exposure to solutions at neutral or basic pH.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.80.17.5181</identifier><identifier>PMID: 6351053</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Amino acids ; Amino Acids - analysis ; Arginine - metabolism ; Biochemistry ; Biosynthesis ; Carboxy-Lyases - genetics ; Carboxy-Lyases - metabolism ; Cell growth ; DNA-binding protein ; Enzymes ; Escherichia coli ; Escherichia coli - enzymology ; Fractions ; histone H2B ; Histones ; Histones - genetics ; Ornithine - metabolism ; Ornithine Decarboxylase - genetics ; Ornithine Decarboxylase - metabolism ; Polyamines ; Polyamines - biosynthesis ; Titration</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1983-09, Vol.80 (17), p.5181-5184</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c492t-eb275ec468294fb474966c64d5d6a2182d0a8098aaff8ef3713deb817ecd36523</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/80/17.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/14083$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/14083$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793,58238,58471</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6351053$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Heller, John S.</creatorcontrib><creatorcontrib>Rostomily, Robert</creatorcontrib><creatorcontrib>Kyriakidis, Dimitri A.</creatorcontrib><creatorcontrib>Canellakis, Evangelos S.</creatorcontrib><title>Regulation of Polyamine Biosynthesis in Escherichia coli by Basic Proteins</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>In Escherichia coli, the biosynthetic ornithine and arginine decarboxylases (EC 4.1.1.17 and 4.1.1.19, respectively) are responsible for the biosynthesis of polyamines from ornithine and arginine, respectively. When E. coli cells are grown in the presence of increasing amounts of polyamines, a progressive increase in the amount of antizyme 1 and antizyme 2 occurs. The amino acid compositions of antizymes 1 and 2 show them to be basic proteins; antizyme 1 has an amino acid composition similar to that of the E. coli histone-like protein HU and of the eukaryotic histone H2B; antizyme 2 is characterized by an unusually high arginine content. We find these proteins to be specific inhibitors of both the biosynthetic ornithine decarboxylase and the biosynthetic arginine decarboxylase. They do not inhibit the corresponding biodegradative ornithine and arginine decarboxylases, nor do they inhibit lysine decarboxylase or S-adenosylmethionine decarboxylase. These properties of the antizymes favor their function in the regulation of polyamine biosynthesis in E. coli. The ability of the purified antizymes to inhibit the ornithine and arginine decarboxylases is stabilized in acidic buffers and is lost upon prolonged exposure to solutions at neutral or basic pH.</description><subject>Amino acids</subject><subject>Amino Acids - analysis</subject><subject>Arginine - metabolism</subject><subject>Biochemistry</subject><subject>Biosynthesis</subject><subject>Carboxy-Lyases - genetics</subject><subject>Carboxy-Lyases - metabolism</subject><subject>Cell growth</subject><subject>DNA-binding protein</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Escherichia coli - enzymology</subject><subject>Fractions</subject><subject>histone H2B</subject><subject>Histones</subject><subject>Histones - genetics</subject><subject>Ornithine - metabolism</subject><subject>Ornithine Decarboxylase - genetics</subject><subject>Ornithine Decarboxylase - metabolism</subject><subject>Polyamines</subject><subject>Polyamines - biosynthesis</subject><subject>Titration</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><recordid>eNqFkUtvEzEUhS0EKqGwRkICeUVXk9pjjx8LFrQqL1WiQrC2PJ47jSvHTu0ZRP49jpK2sIHV1dX5ztG1D0IvKVlSItnpJtqyVHWRy44q-ggtKNG0EVyTx2hBSCsbxVv-FD0r5YYQojtFjtCRYB0lHVugL9_geg528iniNOKrFLZ27SPgM5_KNk4rKL5gH_FFcSvI3q28xS4Fj_stPrPFO3yV0wQ-lufoyWhDgReHeYx-fLj4fv6pufz68fP5-8vGcd1ODfSt7MBxoVrNx55LroVwgg_dIGxLVTsQq4hW1o6jgpFJygboFZXgBia6lh2jd_vczdyvYXAQp2yD2WS_tnlrkvXmbyX6lblOPw2rP0G76n978Od0O0OZzNoXByHYCGkuRhHBNFH_BymTilOpK3i6B11OpWQY74-hxOxqMruaarCh0uxqqo7Xf77hnj_0UvWTg74z3qkPAWacQ5jg11TJN_8kK_BqD9yUKeWHyzhRjP0G-YiwVw</recordid><startdate>19830901</startdate><enddate>19830901</enddate><creator>Heller, John S.</creator><creator>Rostomily, Robert</creator><creator>Kyriakidis, Dimitri A.</creator><creator>Canellakis, Evangelos S.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</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>7QO</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19830901</creationdate><title>Regulation of Polyamine Biosynthesis in Escherichia coli by Basic Proteins</title><author>Heller, John S. ; Rostomily, Robert ; Kyriakidis, Dimitri A. ; Canellakis, Evangelos S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c492t-eb275ec468294fb474966c64d5d6a2182d0a8098aaff8ef3713deb817ecd36523</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>Amino acids</topic><topic>Amino Acids - analysis</topic><topic>Arginine - metabolism</topic><topic>Biochemistry</topic><topic>Biosynthesis</topic><topic>Carboxy-Lyases - genetics</topic><topic>Carboxy-Lyases - metabolism</topic><topic>Cell growth</topic><topic>DNA-binding protein</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>Escherichia coli - enzymology</topic><topic>Fractions</topic><topic>histone H2B</topic><topic>Histones</topic><topic>Histones - genetics</topic><topic>Ornithine - metabolism</topic><topic>Ornithine Decarboxylase - genetics</topic><topic>Ornithine Decarboxylase - metabolism</topic><topic>Polyamines</topic><topic>Polyamines - biosynthesis</topic><topic>Titration</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Heller, John S.</creatorcontrib><creatorcontrib>Rostomily, Robert</creatorcontrib><creatorcontrib>Kyriakidis, Dimitri A.</creatorcontrib><creatorcontrib>Canellakis, Evangelos S.</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>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Heller, John S.</au><au>Rostomily, Robert</au><au>Kyriakidis, Dimitri A.</au><au>Canellakis, Evangelos S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Regulation of Polyamine Biosynthesis in Escherichia coli by Basic Proteins</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1983-09-01</date><risdate>1983</risdate><volume>80</volume><issue>17</issue><spage>5181</spage><epage>5184</epage><pages>5181-5184</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>In Escherichia coli, the biosynthetic ornithine and arginine decarboxylases (EC 4.1.1.17 and 4.1.1.19, respectively) are responsible for the biosynthesis of polyamines from ornithine and arginine, respectively. When E. coli cells are grown in the presence of increasing amounts of polyamines, a progressive increase in the amount of antizyme 1 and antizyme 2 occurs. The amino acid compositions of antizymes 1 and 2 show them to be basic proteins; antizyme 1 has an amino acid composition similar to that of the E. coli histone-like protein HU and of the eukaryotic histone H2B; antizyme 2 is characterized by an unusually high arginine content. We find these proteins to be specific inhibitors of both the biosynthetic ornithine decarboxylase and the biosynthetic arginine decarboxylase. They do not inhibit the corresponding biodegradative ornithine and arginine decarboxylases, nor do they inhibit lysine decarboxylase or S-adenosylmethionine decarboxylase. These properties of the antizymes favor their function in the regulation of polyamine biosynthesis in E. coli. 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subjects | Amino acids Amino Acids - analysis Arginine - metabolism Biochemistry Biosynthesis Carboxy-Lyases - genetics Carboxy-Lyases - metabolism Cell growth DNA-binding protein Enzymes Escherichia coli Escherichia coli - enzymology Fractions histone H2B Histones Histones - genetics Ornithine - metabolism Ornithine Decarboxylase - genetics Ornithine Decarboxylase - metabolism Polyamines Polyamines - biosynthesis Titration |
title | Regulation of Polyamine Biosynthesis in Escherichia coli by Basic Proteins |
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