Prenylcysteine methylesterase in Arabidopsis thaliana
Prenylated proteins undergo a series of post-translational modifications, including prenylation, proteolysis, and methylation. Collectively, these modifications generate a prenylcysteine methylester at the carboxyl terminus and modulate protein targeting and function. Prenylcysteine methylation is t...
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| Veröffentlicht in: | Gene 2006-10, Vol.380 (2), p.159-166 |
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| creator | Deem, Angela K. Bultema, Rebecca L. Crowell, Dring N. |
| description | Prenylated proteins undergo a series of post-translational modifications, including prenylation, proteolysis, and methylation. Collectively, these modifications generate a prenylcysteine methylester at the carboxyl terminus and modulate protein targeting and function. Prenylcysteine methylation is the only reversible step in this series of modifications. However, prenylcysteine α-carboxyl methylesterase (PCME) activity has not been described in plants. We have detected a specific PCME activity in
Arabidopsis thaliana membranes that discriminates between biologically relevant and irrelevant prenylcysteine methylester substrates. Furthermore, we have identified an
Arabidopsis gene (
At5g15860) that encodes measurable PCME activity in recombinant yeast cells with greater specificity for biologically relevant prenylcysteine methylesters than the activity found in
Arabidopsis membranes. These results suggest that specific and non-specific esterases catalyze the demethylation of prenylcysteine methylesters in
Arabidopsis membranes. Our findings are discussed in the context of prenylcysteine methylation/demethylation as a potential regulatory mechanism for membrane association and function of prenylated proteins in
Arabidopsis. |
| doi_str_mv | 10.1016/j.gene.2006.05.023 |
| format | Article |
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Arabidopsis thaliana membranes that discriminates between biologically relevant and irrelevant prenylcysteine methylester substrates. Furthermore, we have identified an
Arabidopsis gene (
At5g15860) that encodes measurable PCME activity in recombinant yeast cells with greater specificity for biologically relevant prenylcysteine methylesters than the activity found in
Arabidopsis membranes. These results suggest that specific and non-specific esterases catalyze the demethylation of prenylcysteine methylesters in
Arabidopsis membranes. Our findings are discussed in the context of prenylcysteine methylation/demethylation as a potential regulatory mechanism for membrane association and function of prenylated proteins in
Arabidopsis.</description><identifier>ISSN: 0378-1119</identifier><identifier>EISSN: 1879-0038</identifier><identifier>DOI: 10.1016/j.gene.2006.05.023</identifier><identifier>PMID: 16870359</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Arabidopsis - cytology ; Arabidopsis - enzymology ; Arabidopsis - genetics ; Arabidopsis Proteins - genetics ; Arabidopsis Proteins - metabolism ; Arabidopsis Proteins - physiology ; Arabidopsis thaliana ; Carboxylic Ester Hydrolases - genetics ; Carboxylic Ester Hydrolases - isolation & purification ; Carboxylic Ester Hydrolases - metabolism ; Cell Membrane - enzymology ; Cloning, Molecular ; Esterases - physiology ; Gene Expression Regulation, Plant ; Methanol - metabolism ; Molecular Sequence Data ; Phylogeny ; Protein methylation ; Protein Methyltransferases - metabolism ; Protein prenylation ; Protein Prenylation - physiology ; Sequence Homology, Amino Acid</subject><ispartof>Gene, 2006-10, Vol.380 (2), p.159-166</ispartof><rights>2006 Elsevier B.V.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c385t-eafb97bb85b996a128b9fcd086058e9ab2a9383521709d570bf24ac89d063fad3</citedby><cites>FETCH-LOGICAL-c385t-eafb97bb85b996a128b9fcd086058e9ab2a9383521709d570bf24ac89d063fad3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0378111906003714$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16870359$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Deem, Angela K.</creatorcontrib><creatorcontrib>Bultema, Rebecca L.</creatorcontrib><creatorcontrib>Crowell, Dring N.</creatorcontrib><title>Prenylcysteine methylesterase in Arabidopsis thaliana</title><title>Gene</title><addtitle>Gene</addtitle><description>Prenylated proteins undergo a series of post-translational modifications, including prenylation, proteolysis, and methylation. Collectively, these modifications generate a prenylcysteine methylester at the carboxyl terminus and modulate protein targeting and function. Prenylcysteine methylation is the only reversible step in this series of modifications. However, prenylcysteine α-carboxyl methylesterase (PCME) activity has not been described in plants. We have detected a specific PCME activity in
Arabidopsis thaliana membranes that discriminates between biologically relevant and irrelevant prenylcysteine methylester substrates. Furthermore, we have identified an
Arabidopsis gene (
At5g15860) that encodes measurable PCME activity in recombinant yeast cells with greater specificity for biologically relevant prenylcysteine methylesters than the activity found in
Arabidopsis membranes. These results suggest that specific and non-specific esterases catalyze the demethylation of prenylcysteine methylesters in
Arabidopsis membranes. Our findings are discussed in the context of prenylcysteine methylation/demethylation as a potential regulatory mechanism for membrane association and function of prenylated proteins in
Arabidopsis.</description><subject>Amino Acid Sequence</subject><subject>Arabidopsis - cytology</subject><subject>Arabidopsis - enzymology</subject><subject>Arabidopsis - genetics</subject><subject>Arabidopsis Proteins - genetics</subject><subject>Arabidopsis Proteins - metabolism</subject><subject>Arabidopsis Proteins - physiology</subject><subject>Arabidopsis thaliana</subject><subject>Carboxylic Ester Hydrolases - genetics</subject><subject>Carboxylic Ester Hydrolases - isolation & purification</subject><subject>Carboxylic Ester Hydrolases - metabolism</subject><subject>Cell Membrane - enzymology</subject><subject>Cloning, Molecular</subject><subject>Esterases - physiology</subject><subject>Gene Expression Regulation, Plant</subject><subject>Methanol - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Phylogeny</subject><subject>Protein methylation</subject><subject>Protein Methyltransferases - metabolism</subject><subject>Protein prenylation</subject><subject>Protein Prenylation - physiology</subject><subject>Sequence Homology, Amino Acid</subject><issn>0378-1119</issn><issn>1879-0038</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LAzEQhoMotlb_gAfpyduuk6TZTcBLKX5BQQ96Dkl21qZsd2uyFfbfm9KCN53LMPDMO8NDyDWFnAIt7tb5J7aYM4AiB5ED4ydkTGWpMgAuT8kYeCkzSqkakYsY15BKCHZORrSQJXChxkS8BWyHxg2xR9_idIP9amgwTcFEnPp2Og_G-qrbRh-n_co03rTmkpzVpol4dewT8vH48L54zpavTy-L-TJzXIo-Q1NbVVorhVWqMJRJq2pXgSxASFTGMqO45ILRElQlSrA1mxknVQUFr03FJ-T2kLsN3dcufaU3PjpsGtNit4u6kLIoGZ39C9J0B4CyBLID6EIXY8Bab4PfmDBoCnpvVa_13qreW9UgdLKalm6O6Tu7wep35agxAfcHAJOMb49BR-exdVj5gK7XVef_yv8BOQ6Iew</recordid><startdate>20061001</startdate><enddate>20061001</enddate><creator>Deem, Angela K.</creator><creator>Bultema, Rebecca L.</creator><creator>Crowell, Dring N.</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>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20061001</creationdate><title>Prenylcysteine methylesterase in Arabidopsis thaliana</title><author>Deem, Angela K. ; Bultema, Rebecca L. ; Crowell, Dring N.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c385t-eafb97bb85b996a128b9fcd086058e9ab2a9383521709d570bf24ac89d063fad3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Amino Acid Sequence</topic><topic>Arabidopsis - cytology</topic><topic>Arabidopsis - enzymology</topic><topic>Arabidopsis - genetics</topic><topic>Arabidopsis Proteins - genetics</topic><topic>Arabidopsis Proteins - metabolism</topic><topic>Arabidopsis Proteins - physiology</topic><topic>Arabidopsis thaliana</topic><topic>Carboxylic Ester Hydrolases - genetics</topic><topic>Carboxylic Ester Hydrolases - isolation & purification</topic><topic>Carboxylic Ester Hydrolases - metabolism</topic><topic>Cell Membrane - enzymology</topic><topic>Cloning, Molecular</topic><topic>Esterases - physiology</topic><topic>Gene Expression Regulation, Plant</topic><topic>Methanol - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Phylogeny</topic><topic>Protein methylation</topic><topic>Protein Methyltransferases - metabolism</topic><topic>Protein prenylation</topic><topic>Protein Prenylation - physiology</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Deem, Angela K.</creatorcontrib><creatorcontrib>Bultema, Rebecca L.</creatorcontrib><creatorcontrib>Crowell, Dring N.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</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>Deem, Angela K.</au><au>Bultema, Rebecca L.</au><au>Crowell, Dring N.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Prenylcysteine methylesterase in Arabidopsis thaliana</atitle><jtitle>Gene</jtitle><addtitle>Gene</addtitle><date>2006-10-01</date><risdate>2006</risdate><volume>380</volume><issue>2</issue><spage>159</spage><epage>166</epage><pages>159-166</pages><issn>0378-1119</issn><eissn>1879-0038</eissn><abstract>Prenylated proteins undergo a series of post-translational modifications, including prenylation, proteolysis, and methylation. Collectively, these modifications generate a prenylcysteine methylester at the carboxyl terminus and modulate protein targeting and function. Prenylcysteine methylation is the only reversible step in this series of modifications. However, prenylcysteine α-carboxyl methylesterase (PCME) activity has not been described in plants. We have detected a specific PCME activity in
Arabidopsis thaliana membranes that discriminates between biologically relevant and irrelevant prenylcysteine methylester substrates. Furthermore, we have identified an
Arabidopsis gene (
At5g15860) that encodes measurable PCME activity in recombinant yeast cells with greater specificity for biologically relevant prenylcysteine methylesters than the activity found in
Arabidopsis membranes. These results suggest that specific and non-specific esterases catalyze the demethylation of prenylcysteine methylesters in
Arabidopsis membranes. Our findings are discussed in the context of prenylcysteine methylation/demethylation as a potential regulatory mechanism for membrane association and function of prenylated proteins in
Arabidopsis.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>16870359</pmid><doi>10.1016/j.gene.2006.05.023</doi><tpages>8</tpages></addata></record> |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Amino Acid Sequence Arabidopsis - cytology Arabidopsis - enzymology Arabidopsis - genetics Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Arabidopsis Proteins - physiology Arabidopsis thaliana Carboxylic Ester Hydrolases - genetics Carboxylic Ester Hydrolases - isolation & purification Carboxylic Ester Hydrolases - metabolism Cell Membrane - enzymology Cloning, Molecular Esterases - physiology Gene Expression Regulation, Plant Methanol - metabolism Molecular Sequence Data Phylogeny Protein methylation Protein Methyltransferases - metabolism Protein prenylation Protein Prenylation - physiology Sequence Homology, Amino Acid |
| title | Prenylcysteine methylesterase in Arabidopsis thaliana |
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