Molecular Characterization of Ethylene Response Sensor 1 (BoERS1) in Bambusa oldhamii
An ethylene receptor gene named BoERS1 was cloned from a bamboo (Bambusa oldhamii) cDNA library. The open reading frame of BoERS1 was 1,899 bp and encoded a 632-amino acid protein, which contains the five conserved motifs (H, N, G1, F, and G2 boxes) of the bacterial two-component system histidine ki...
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| Veröffentlicht in: | Plant molecular biology reporter 2016-04, Vol.34 (2), p.387-398 |
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| creator | Hsieh, Yi-Lin Lu, Ching-Fang Chiang, Bing-Yu Liao, Shu-Chien Chen, Rita P.-Y Lin, Choun-Sea Wang, Ai-Yu Yang, Chien-Chih |
| description | An ethylene receptor gene named BoERS1 was cloned from a bamboo (Bambusa oldhamii) cDNA library. The open reading frame of BoERS1 was 1,899 bp and encoded a 632-amino acid protein, which contains the five conserved motifs (H, N, G1, F, and G2 boxes) of the bacterial two-component system histidine kinases and shows high sequence similarity with other ethylene receptors in plants, such as rice and maize. Expression of BoERS1 in bamboo shoots increased with the growth of the emerging shoots. In an in vitro kinase assay, the expressed histidine kinase domain of BoERS1 (BHK) was phosphorylated in the presence of Mn²⁺, and LC-ESI-MS/MS analysis showed that four amino acids, namely T442, S444, S489, and S503, were phosphorylated. It is interesting to note that S489 and S503 are located in a loop region (L1) that is found only in plant histidine kinase-containing enzymes. The identification of multiple phosphorylation sites on BoERS1 provides a new avenue for future structure–function studies of the ethylene receptor protein family. |
| doi_str_mv | 10.1007/s11105-015-0929-z |
| format | Article |
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The open reading frame of BoERS1 was 1,899 bp and encoded a 632-amino acid protein, which contains the five conserved motifs (H, N, G1, F, and G2 boxes) of the bacterial two-component system histidine kinases and shows high sequence similarity with other ethylene receptors in plants, such as rice and maize. Expression of BoERS1 in bamboo shoots increased with the growth of the emerging shoots. In an in vitro kinase assay, the expressed histidine kinase domain of BoERS1 (BHK) was phosphorylated in the presence of Mn²⁺, and LC-ESI-MS/MS analysis showed that four amino acids, namely T442, S444, S489, and S503, were phosphorylated. It is interesting to note that S489 and S503 are located in a loop region (L1) that is found only in plant histidine kinase-containing enzymes. The identification of multiple phosphorylation sites on BoERS1 provides a new avenue for future structure–function studies of the ethylene receptor protein family.</description><identifier>ISSN: 0735-9640</identifier><identifier>EISSN: 1572-9818</identifier><identifier>DOI: 10.1007/s11105-015-0929-z</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Amino acids ; bamboo shoots ; bamboos ; Bambusa oldhamii ; Bioinformatics ; Biomedical and Life Sciences ; cDNA libraries ; complementary DNA ; corn ; ethylene ; genes ; histidine ; histidine kinase ; Life Sciences ; manganese ; Metabolomics ; open reading frames ; Original Paper ; phosphorylation ; Plant biology ; Plant Breeding/Biotechnology ; Plant Sciences ; Proteomics ; receptors ; rice ; sequence homology ; shoots</subject><ispartof>Plant molecular biology reporter, 2016-04, Vol.34 (2), p.387-398</ispartof><rights>Springer Science+Business Media New York 2015</rights><rights>Springer Science+Business Media New York 2016</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c292t-6735828e8b92831382c8d2ff0387290d841512bf18aa10489b605722b8e1ebdc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s11105-015-0929-z$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11105-015-0929-z$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids></links><search><creatorcontrib>Hsieh, Yi-Lin</creatorcontrib><creatorcontrib>Lu, Ching-Fang</creatorcontrib><creatorcontrib>Chiang, Bing-Yu</creatorcontrib><creatorcontrib>Liao, Shu-Chien</creatorcontrib><creatorcontrib>Chen, Rita P.-Y</creatorcontrib><creatorcontrib>Lin, Choun-Sea</creatorcontrib><creatorcontrib>Wang, Ai-Yu</creatorcontrib><creatorcontrib>Yang, Chien-Chih</creatorcontrib><title>Molecular Characterization of Ethylene Response Sensor 1 (BoERS1) in Bambusa oldhamii</title><title>Plant molecular biology reporter</title><addtitle>Plant Mol Biol Rep</addtitle><description>An ethylene receptor gene named BoERS1 was cloned from a bamboo (Bambusa oldhamii) cDNA library. The open reading frame of BoERS1 was 1,899 bp and encoded a 632-amino acid protein, which contains the five conserved motifs (H, N, G1, F, and G2 boxes) of the bacterial two-component system histidine kinases and shows high sequence similarity with other ethylene receptors in plants, such as rice and maize. Expression of BoERS1 in bamboo shoots increased with the growth of the emerging shoots. In an in vitro kinase assay, the expressed histidine kinase domain of BoERS1 (BHK) was phosphorylated in the presence of Mn²⁺, and LC-ESI-MS/MS analysis showed that four amino acids, namely T442, S444, S489, and S503, were phosphorylated. It is interesting to note that S489 and S503 are located in a loop region (L1) that is found only in plant histidine kinase-containing enzymes. The identification of multiple phosphorylation sites on BoERS1 provides a new avenue for future structure–function studies of the ethylene receptor protein family.</description><subject>Amino acids</subject><subject>bamboo shoots</subject><subject>bamboos</subject><subject>Bambusa oldhamii</subject><subject>Bioinformatics</subject><subject>Biomedical and Life Sciences</subject><subject>cDNA libraries</subject><subject>complementary DNA</subject><subject>corn</subject><subject>ethylene</subject><subject>genes</subject><subject>histidine</subject><subject>histidine kinase</subject><subject>Life Sciences</subject><subject>manganese</subject><subject>Metabolomics</subject><subject>open reading frames</subject><subject>Original Paper</subject><subject>phosphorylation</subject><subject>Plant biology</subject><subject>Plant Breeding/Biotechnology</subject><subject>Plant Sciences</subject><subject>Proteomics</subject><subject>receptors</subject><subject>rice</subject><subject>sequence homology</subject><subject>shoots</subject><issn>0735-9640</issn><issn>1572-9818</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>BENPR</sourceid><recordid>eNp9kD1PwzAQhi0EEqXwA5iwxAJD4M5JmvMIVfmQipBaOltO6rSp0rjYydD-elyFgYnhdMv73MfD2DXCAwJkjx4RIY0AQ0kho8MJG2CaiUgS0ikbQBankRwlcM4uvN9AYIBowBYftjZFV2vHx2vtdNEaVx10W9mG25JP2vW-No3hM-N3tvGGz03jrePI757tZDbHe141_Flv885rbuvlWm-r6pKdlbr25uq3D9niZfI1foumn6_v46dpVAgp2mgUjiJBhnIpKMaYREFLUZYQUyYkLCnBFEVeImmNkJDMRxB-EjkZNPmyiIfstp-7c_a7M75VG9u5JqxUmGWJkARxElLYpwpnvXemVDtXbbXbKwR1tKd6eyrYU0d76hAY0TM-ZJuVcX8m_wPd9FCprdIrV3m1mAvAEQAKSuM0_gFcO3mR</recordid><startdate>20160401</startdate><enddate>20160401</enddate><creator>Hsieh, Yi-Lin</creator><creator>Lu, Ching-Fang</creator><creator>Chiang, Bing-Yu</creator><creator>Liao, Shu-Chien</creator><creator>Chen, Rita P.-Y</creator><creator>Lin, Choun-Sea</creator><creator>Wang, Ai-Yu</creator><creator>Yang, Chien-Chih</creator><general>Springer US</general><general>Springer Nature B.V</general><scope>FBQ</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7QR</scope><scope>7T7</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FK</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>LK8</scope><scope>M0K</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope></search><sort><creationdate>20160401</creationdate><title>Molecular Characterization of Ethylene Response Sensor 1 (BoERS1) in Bambusa oldhamii</title><author>Hsieh, Yi-Lin ; 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The open reading frame of BoERS1 was 1,899 bp and encoded a 632-amino acid protein, which contains the five conserved motifs (H, N, G1, F, and G2 boxes) of the bacterial two-component system histidine kinases and shows high sequence similarity with other ethylene receptors in plants, such as rice and maize. Expression of BoERS1 in bamboo shoots increased with the growth of the emerging shoots. In an in vitro kinase assay, the expressed histidine kinase domain of BoERS1 (BHK) was phosphorylated in the presence of Mn²⁺, and LC-ESI-MS/MS analysis showed that four amino acids, namely T442, S444, S489, and S503, were phosphorylated. It is interesting to note that S489 and S503 are located in a loop region (L1) that is found only in plant histidine kinase-containing enzymes. The identification of multiple phosphorylation sites on BoERS1 provides a new avenue for future structure–function studies of the ethylene receptor protein family.</abstract><cop>New York</cop><pub>Springer US</pub><doi>10.1007/s11105-015-0929-z</doi><tpages>12</tpages></addata></record> |
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| subjects | Amino acids bamboo shoots bamboos Bambusa oldhamii Bioinformatics Biomedical and Life Sciences cDNA libraries complementary DNA corn ethylene genes histidine histidine kinase Life Sciences manganese Metabolomics open reading frames Original Paper phosphorylation Plant biology Plant Breeding/Biotechnology Plant Sciences Proteomics receptors rice sequence homology shoots |
| title | Molecular Characterization of Ethylene Response Sensor 1 (BoERS1) in Bambusa oldhamii |
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