Regulation of CAX1, an Arabidopsis Ca(2+)/H+ antiporter. Identification of an N-terminal autoinhibitory domain
Regulation of Ca(2+) transport determines the duration of a Ca(2+) signal, and hence, the nature of the biological response. Ca(2+)/H+ antiporters such as CAX1 (cation exchanger 1), play a key role in determining cytosolic Ca(2+) levels. Analysis of a full-length CAX1 clone suggested that the CAX1 o...
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| Veröffentlicht in: | Plant physiology (Bethesda) 2001-11, Vol.127 (3), p.1020-1029 |
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| container_end_page | 1029 |
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| container_title | Plant physiology (Bethesda) |
| container_volume | 127 |
| creator | Pittman, J K Hirschi, K D |
| description | Regulation of Ca(2+) transport determines the duration of a Ca(2+) signal, and hence, the nature of the biological response. Ca(2+)/H+ antiporters such as CAX1 (cation exchanger 1), play a key role in determining cytosolic Ca(2+) levels. Analysis of a full-length CAX1 clone suggested that the CAX1 open reading frame contains an additional 36 amino acids at the N terminus that were not found in the original clone identified by suppression of yeast (Saccharomyces cerevisiae) vacuolar Ca(2+) transport mutants. The long CAX1 (lCAX1) could not suppress the yeast Ca(2+) transport defects despite localization to the yeast vacuole. Calmodulin could not stimulate lCAX1 Ca(2+)/H+ transport in yeast; however, minor alterations in the 36-amino acid region restored Ca(2+)/H+ transport. Sequence analysis suggests that a 36-amino acid N-terminal regulatory domain may be present in all Arabidopsis CAX-like genes. Together, these results suggest a structural feature involved in regulation of Ca(2+)/H+ antiport. |
| doi_str_mv | 10.1104/pp.010409 |
| format | Article |
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The long CAX1 (lCAX1) could not suppress the yeast Ca(2+) transport defects despite localization to the yeast vacuole. Calmodulin could not stimulate lCAX1 Ca(2+)/H+ transport in yeast; however, minor alterations in the 36-amino acid region restored Ca(2+)/H+ transport. Sequence analysis suggests that a 36-amino acid N-terminal regulatory domain may be present in all Arabidopsis CAX-like genes. Together, these results suggest a structural feature involved in regulation of Ca(2+)/H+ antiport.</description><identifier>ISSN: 0032-0889</identifier><identifier>DOI: 10.1104/pp.010409</identifier><identifier>PMID: 11706183</identifier><language>eng</language><publisher>United States</publisher><subject>Amino Acid Sequence ; Antiporters - genetics ; Antiporters - metabolism ; Arabidopsis - genetics ; Arabidopsis - metabolism ; Arabidopsis Proteins - genetics ; Arabidopsis Proteins - metabolism ; Calcium - metabolism ; Calcium-Binding Proteins - genetics ; Calcium-Binding Proteins - metabolism ; Cation Transport Proteins ; Chromosome Mapping ; Cytosol - metabolism ; Hydrogen - metabolism ; Hydrogen-Ion Concentration ; Ion Transport ; Molecular Sequence Data ; Protein Structure, Tertiary ; Saccharomyces cerevisiae - metabolism ; Sequence Homology, Amino Acid ; Signal Transduction ; Vacuoles - metabolism</subject><ispartof>Plant physiology (Bethesda), 2001-11, Vol.127 (3), p.1020-1029</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11706183$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pittman, J K</creatorcontrib><creatorcontrib>Hirschi, K D</creatorcontrib><title>Regulation of CAX1, an Arabidopsis Ca(2+)/H+ antiporter. Identification of an N-terminal autoinhibitory domain</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>Regulation of Ca(2+) transport determines the duration of a Ca(2+) signal, and hence, the nature of the biological response. Ca(2+)/H+ antiporters such as CAX1 (cation exchanger 1), play a key role in determining cytosolic Ca(2+) levels. Analysis of a full-length CAX1 clone suggested that the CAX1 open reading frame contains an additional 36 amino acids at the N terminus that were not found in the original clone identified by suppression of yeast (Saccharomyces cerevisiae) vacuolar Ca(2+) transport mutants. The long CAX1 (lCAX1) could not suppress the yeast Ca(2+) transport defects despite localization to the yeast vacuole. Calmodulin could not stimulate lCAX1 Ca(2+)/H+ transport in yeast; however, minor alterations in the 36-amino acid region restored Ca(2+)/H+ transport. Sequence analysis suggests that a 36-amino acid N-terminal regulatory domain may be present in all Arabidopsis CAX-like genes. Together, these results suggest a structural feature involved in regulation of Ca(2+)/H+ antiport.</description><subject>Amino Acid Sequence</subject><subject>Antiporters - genetics</subject><subject>Antiporters - metabolism</subject><subject>Arabidopsis - genetics</subject><subject>Arabidopsis - metabolism</subject><subject>Arabidopsis Proteins - genetics</subject><subject>Arabidopsis Proteins - metabolism</subject><subject>Calcium - metabolism</subject><subject>Calcium-Binding Proteins - genetics</subject><subject>Calcium-Binding Proteins - metabolism</subject><subject>Cation Transport Proteins</subject><subject>Chromosome Mapping</subject><subject>Cytosol - metabolism</subject><subject>Hydrogen - metabolism</subject><subject>Hydrogen-Ion Concentration</subject><subject>Ion Transport</subject><subject>Molecular Sequence Data</subject><subject>Protein Structure, Tertiary</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Signal Transduction</subject><subject>Vacuoles - metabolism</subject><issn>0032-0889</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kMFLwzAYxXNQ3Jwe_AckJ3HMbt-XdE17HEXdYCiIgreSNqlG2iY27WH_vQGnp8fjvd87PEKuEJaIEK-cW0JQyE7IFICzCNI0m5Bz778AADnGZ2SCKCDBlE9J96I_xkYOxnbU1jTfvOMdlR3d9LI0yjpvPM3lLVvMV9tFCAbjbD_ofkl3SgdXm-ofDthTFLLWdLKhchys6T5NaQbbH6iyrTTdBTmtZeP15VFn5O3h_jXfRvvnx12-2UcOGRsiliVMJCrOdMxKhJorSKpYJ5lKFZYgOGqWCi3XqWAM42zNs5qLNYhEQ1xJyWfk5nfX9fZ71H4oWuMr3TSy03b0RcAEBjgUr4_FsWy1KlxvWtkfir-H-A_UBmMv</recordid><startdate>200111</startdate><enddate>200111</enddate><creator>Pittman, J K</creator><creator>Hirschi, K D</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>200111</creationdate><title>Regulation of CAX1, an Arabidopsis Ca(2+)/H+ antiporter. 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Calmodulin could not stimulate lCAX1 Ca(2+)/H+ transport in yeast; however, minor alterations in the 36-amino acid region restored Ca(2+)/H+ transport. Sequence analysis suggests that a 36-amino acid N-terminal regulatory domain may be present in all Arabidopsis CAX-like genes. Together, these results suggest a structural feature involved in regulation of Ca(2+)/H+ antiport.</abstract><cop>United States</cop><pmid>11706183</pmid><doi>10.1104/pp.010409</doi><tpages>10</tpages></addata></record> |
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| ispartof | Plant physiology (Bethesda), 2001-11, Vol.127 (3), p.1020-1029 |
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| language | eng |
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| source | Jstor Complete Legacy; Oxford University Press Journals All Titles (1996-Current); MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Amino Acid Sequence Antiporters - genetics Antiporters - metabolism Arabidopsis - genetics Arabidopsis - metabolism Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Calcium - metabolism Calcium-Binding Proteins - genetics Calcium-Binding Proteins - metabolism Cation Transport Proteins Chromosome Mapping Cytosol - metabolism Hydrogen - metabolism Hydrogen-Ion Concentration Ion Transport Molecular Sequence Data Protein Structure, Tertiary Saccharomyces cerevisiae - metabolism Sequence Homology, Amino Acid Signal Transduction Vacuoles - metabolism |
| title | Regulation of CAX1, an Arabidopsis Ca(2+)/H+ antiporter. Identification of an N-terminal autoinhibitory domain |
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