Drosophila protein kinase CK2 is rendered temperature-sensitive by mutations of highly conserved residues flanking the activation segment
CK2 is a Ser/Thr protein kinase essential for animal development. Although null alleles for CK2 are available in the mouse and Drosophila models, they are lethal when homozygous, thus necessitating conditional alleles for analysis of its developmental roles. We describe the isolation of temperature-...
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| Veröffentlicht in: | Molecular and cellular biochemistry 2009-03, Vol.323 (1-2), p.49-60 |
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| creator | Kuntamalla, Pallavi P Kunttas-Tatli, Ezgi Karandikar, Umesh Bishop, Clifton P Bidwai, Ashok P |
| description | CK2 is a Ser/Thr protein kinase essential for animal development. Although null alleles for CK2 are available in the mouse and Drosophila models, they are lethal when homozygous, thus necessitating conditional alleles for analysis of its developmental roles. We describe the isolation of temperature-sensitive (ts) alleles of Drosophila CK2α (dCK2α). These alleles efficiently rescue lethality of yeast lacking endogenous CK2 at 29°C, but this ability is lost at higher temperatures in an allele-specific manner. These ts-variants exhibit properties akin to the wild type protein, and interact robustly with dCK2β. Modeling of these ts-variants using the crystal structure of human CK2α indicates that the affected residues are in close proximity to the active site. We find that substitution of Asp²¹² elicits potent ts-behavior, an important finding because this residue contributes to stability of the activation segment and is invariant in other Ser/Thr protein kinases. |
| doi_str_mv | 10.1007/s11010-008-9963-6 |
| format | Article |
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Although null alleles for CK2 are available in the mouse and Drosophila models, they are lethal when homozygous, thus necessitating conditional alleles for analysis of its developmental roles. We describe the isolation of temperature-sensitive (ts) alleles of Drosophila CK2α (dCK2α). These alleles efficiently rescue lethality of yeast lacking endogenous CK2 at 29°C, but this ability is lost at higher temperatures in an allele-specific manner. These ts-variants exhibit properties akin to the wild type protein, and interact robustly with dCK2β. Modeling of these ts-variants using the crystal structure of human CK2α indicates that the affected residues are in close proximity to the active site. We find that substitution of Asp²¹² elicits potent ts-behavior, an important finding because this residue contributes to stability of the activation segment and is invariant in other Ser/Thr protein kinases.</description><identifier>ISSN: 0300-8177</identifier><identifier>EISSN: 1573-4919</identifier><identifier>DOI: 10.1007/s11010-008-9963-6</identifier><identifier>PMID: 19039653</identifier><language>eng</language><publisher>Boston: Boston : Springer US</publisher><subject>Amino Acid Sequence ; Animals ; Biochemistry ; Biomedical and Life Sciences ; Cardiology ; Casein Kinase II - chemistry ; Casein Kinase II - genetics ; Casein Kinase II - metabolism ; Drosophila ; Drosophila melanogaster - enzymology ; Drosophila melanogaster - genetics ; Drosophila Proteins - chemistry ; Drosophila Proteins - genetics ; Drosophila Proteins - metabolism ; Enzyme Activation ; High temperature ; Humans ; Insects ; Kinases ; Life Sciences ; Medical Biochemistry ; Mice ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Oncology ; Protein Conformation ; Proteins ; Sequence Alignment ; Temperature ; Yeasts</subject><ispartof>Molecular and cellular biochemistry, 2009-03, Vol.323 (1-2), p.49-60</ispartof><rights>Springer Science+Business Media, LLC. 2008</rights><rights>Springer Science+Business Media, LLC. 2009</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c523t-828a0a5e9c64fa131f6fc75e86cc5fa14f05bae595e94b4bd2283b2962ecea2b3</citedby><cites>FETCH-LOGICAL-c523t-828a0a5e9c64fa131f6fc75e86cc5fa14f05bae595e94b4bd2283b2962ecea2b3</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/s11010-008-9963-6$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11010-008-9963-6$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>230,314,776,780,881,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19039653$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kuntamalla, Pallavi P</creatorcontrib><creatorcontrib>Kunttas-Tatli, Ezgi</creatorcontrib><creatorcontrib>Karandikar, Umesh</creatorcontrib><creatorcontrib>Bishop, Clifton P</creatorcontrib><creatorcontrib>Bidwai, Ashok P</creatorcontrib><title>Drosophila protein kinase CK2 is rendered temperature-sensitive by mutations of highly conserved residues flanking the activation segment</title><title>Molecular and cellular biochemistry</title><addtitle>Mol Cell Biochem</addtitle><addtitle>Mol Cell Biochem</addtitle><description>CK2 is a Ser/Thr protein kinase essential for animal development. Although null alleles for CK2 are available in the mouse and Drosophila models, they are lethal when homozygous, thus necessitating conditional alleles for analysis of its developmental roles. We describe the isolation of temperature-sensitive (ts) alleles of Drosophila CK2α (dCK2α). These alleles efficiently rescue lethality of yeast lacking endogenous CK2 at 29°C, but this ability is lost at higher temperatures in an allele-specific manner. These ts-variants exhibit properties akin to the wild type protein, and interact robustly with dCK2β. Modeling of these ts-variants using the crystal structure of human CK2α indicates that the affected residues are in close proximity to the active site. We find that substitution of Asp²¹² elicits potent ts-behavior, an important finding because this residue contributes to stability of the activation segment and is invariant in other Ser/Thr protein kinases.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Cardiology</subject><subject>Casein Kinase II - chemistry</subject><subject>Casein Kinase II - genetics</subject><subject>Casein Kinase II - metabolism</subject><subject>Drosophila</subject><subject>Drosophila melanogaster - enzymology</subject><subject>Drosophila melanogaster - genetics</subject><subject>Drosophila Proteins - chemistry</subject><subject>Drosophila Proteins - genetics</subject><subject>Drosophila Proteins - metabolism</subject><subject>Enzyme Activation</subject><subject>High temperature</subject><subject>Humans</subject><subject>Insects</subject><subject>Kinases</subject><subject>Life Sciences</subject><subject>Medical Biochemistry</subject><subject>Mice</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Oncology</subject><subject>Protein Conformation</subject><subject>Proteins</subject><subject>Sequence Alignment</subject><subject>Temperature</subject><subject>Yeasts</subject><issn>0300-8177</issn><issn>1573-4919</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNp9ks1u1DAUhSMEotPCA7ABi0VZBfwTJ_EGCQ2_ohIL6NpynJvEJbGndjLSPAJvzW0zgsKiK8v2d4597z1Z9ozR14zS6k1ijDKaU1rnSpUiLx9kGyYrkReKqYfZhgpK85pV1Ul2mtIVRZgy9jg7YYoKVUqxyX69jyGF3eBGQ3YxzOA8-em8SUC2XzlxiUTwLURoyQzTDqKZlwh5Ap_c7PZAmgOZltnMLvhEQkcG1w_jgVjcQtyjLEJy7QKJdKPxaN2TeQBiLKpvVSRBP4Gfn2SPOjMmeHpcz7LLjx9-bD_nF98-fdm-u8it5GLOa14baiQoWxadYYJ1ZWcrCXVprcSDoqOyMSAVIkVTNC3ntWi4KjlYMLwRZ9nb1Xe3NBO0Fp-OZtS76CYTDzoYp_-98W7QfdhrXlVVSWs0eHU0iOEaC5v15JKFEcuDsCRdCYHtL27J83tJzgTnOB4EX_4HXoUlemyDZqqShaxVgRBbIYsjSxG6P39mVN_kQa950JgHfZMHXaLm-d1i_yqOAUCAr0DCK99DvPPyPa4vVlFngjZ9dElffueUCcqkohJtfwN69s34</recordid><startdate>20090301</startdate><enddate>20090301</enddate><creator>Kuntamalla, Pallavi P</creator><creator>Kunttas-Tatli, Ezgi</creator><creator>Karandikar, Umesh</creator><creator>Bishop, Clifton P</creator><creator>Bidwai, Ashok P</creator><general>Boston : Springer US</general><general>Springer US</general><general>Springer Nature B.V</general><scope>FBQ</scope><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>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7T5</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</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>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7SS</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20090301</creationdate><title>Drosophila protein kinase CK2 is rendered temperature-sensitive by mutations of highly conserved residues flanking the activation segment</title><author>Kuntamalla, Pallavi P ; Kunttas-Tatli, Ezgi ; Karandikar, Umesh ; Bishop, Clifton P ; Bidwai, Ashok P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c523t-828a0a5e9c64fa131f6fc75e86cc5fa14f05bae595e94b4bd2283b2962ecea2b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Cardiology</topic><topic>Casein Kinase II - chemistry</topic><topic>Casein Kinase II - genetics</topic><topic>Casein Kinase II - metabolism</topic><topic>Drosophila</topic><topic>Drosophila melanogaster - enzymology</topic><topic>Drosophila melanogaster - genetics</topic><topic>Drosophila Proteins - chemistry</topic><topic>Drosophila Proteins - genetics</topic><topic>Drosophila Proteins - metabolism</topic><topic>Enzyme Activation</topic><topic>High temperature</topic><topic>Humans</topic><topic>Insects</topic><topic>Kinases</topic><topic>Life Sciences</topic><topic>Medical Biochemistry</topic><topic>Mice</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>Oncology</topic><topic>Protein Conformation</topic><topic>Proteins</topic><topic>Sequence Alignment</topic><topic>Temperature</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kuntamalla, Pallavi P</creatorcontrib><creatorcontrib>Kunttas-Tatli, Ezgi</creatorcontrib><creatorcontrib>Karandikar, Umesh</creatorcontrib><creatorcontrib>Bishop, Clifton P</creatorcontrib><creatorcontrib>Bidwai, Ashok P</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Molecular and cellular biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kuntamalla, Pallavi P</au><au>Kunttas-Tatli, Ezgi</au><au>Karandikar, Umesh</au><au>Bishop, Clifton P</au><au>Bidwai, Ashok P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Drosophila protein kinase CK2 is rendered temperature-sensitive by mutations of highly conserved residues flanking the activation segment</atitle><jtitle>Molecular and cellular biochemistry</jtitle><stitle>Mol Cell Biochem</stitle><addtitle>Mol Cell Biochem</addtitle><date>2009-03-01</date><risdate>2009</risdate><volume>323</volume><issue>1-2</issue><spage>49</spage><epage>60</epage><pages>49-60</pages><issn>0300-8177</issn><eissn>1573-4919</eissn><abstract>CK2 is a Ser/Thr protein kinase essential for animal development. Although null alleles for CK2 are available in the mouse and Drosophila models, they are lethal when homozygous, thus necessitating conditional alleles for analysis of its developmental roles. We describe the isolation of temperature-sensitive (ts) alleles of Drosophila CK2α (dCK2α). These alleles efficiently rescue lethality of yeast lacking endogenous CK2 at 29°C, but this ability is lost at higher temperatures in an allele-specific manner. These ts-variants exhibit properties akin to the wild type protein, and interact robustly with dCK2β. Modeling of these ts-variants using the crystal structure of human CK2α indicates that the affected residues are in close proximity to the active site. We find that substitution of Asp²¹² elicits potent ts-behavior, an important finding because this residue contributes to stability of the activation segment and is invariant in other Ser/Thr protein kinases.</abstract><cop>Boston</cop><pub>Boston : Springer US</pub><pmid>19039653</pmid><doi>10.1007/s11010-008-9963-6</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Molecular and cellular biochemistry, 2009-03, Vol.323 (1-2), p.49-60 |
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| subjects | Amino Acid Sequence Animals Biochemistry Biomedical and Life Sciences Cardiology Casein Kinase II - chemistry Casein Kinase II - genetics Casein Kinase II - metabolism Drosophila Drosophila melanogaster - enzymology Drosophila melanogaster - genetics Drosophila Proteins - chemistry Drosophila Proteins - genetics Drosophila Proteins - metabolism Enzyme Activation High temperature Humans Insects Kinases Life Sciences Medical Biochemistry Mice Models, Molecular Molecular Sequence Data Mutation Oncology Protein Conformation Proteins Sequence Alignment Temperature Yeasts |
| title | Drosophila protein kinase CK2 is rendered temperature-sensitive by mutations of highly conserved residues flanking the activation segment |
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