A single point mutation resulting in an adversely reduced expression of DPM2 in the Lec15.1 cells
Mammalian dolichol–phosphate–mannose (DPM) synthase consists of three subunits, DPM1, DPM2, and DPM3. Lec15.1 Chinese hamster ovary cells are deficient in DPM synthase activity. The present paper reports that DPM1 cDNA from wild type and Lec15.1 CHO cells were found to be identical, and transfection...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2003-12, Vol.312 (3), p.555-561 |
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| creator | Pu, Lixia Scocca, Jane R Walker, Brian K Krag, Sharon S |
| description | Mammalian dolichol–phosphate–mannose (DPM) synthase consists of three subunits, DPM1, DPM2, and DPM3. Lec15.1 Chinese hamster ovary cells are deficient in DPM synthase activity. The present paper reports that DPM1 cDNA from wild type and Lec15.1 CHO cells were found to be identical, and transfection with CHO DPM1 cDNA did not reverse the Lec15.1 phenotype. Neither did a chimeric cDNA containing the complete hamster DPM1 open reading frame fused to the
Saccharomyces cerevisiae DPM1 C-terminal transmembrane domain. In contrast, Lec15.1 cells were found to have a single point mutation G29A within the coding region of the
DPM2 gene, resulting in a glycine to glutamic acid change in amino acid residue 10 of the peptide. Moreover, mutant DPM2 cDNA expressed a drastically reduced amount of DPM2 protein and poorly corrects the Lec15.1 cell phenotype when compared with wild type CHO DPM2 cDNA (G
29 form). |
| doi_str_mv | 10.1016/j.bbrc.2003.10.152 |
| format | Article |
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Saccharomyces cerevisiae DPM1 C-terminal transmembrane domain. In contrast, Lec15.1 cells were found to have a single point mutation G29A within the coding region of the
DPM2 gene, resulting in a glycine to glutamic acid change in amino acid residue 10 of the peptide. Moreover, mutant DPM2 cDNA expressed a drastically reduced amount of DPM2 protein and poorly corrects the Lec15.1 cell phenotype when compared with wild type CHO DPM2 cDNA (G
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Saccharomyces cerevisiae DPM1 C-terminal transmembrane domain. In contrast, Lec15.1 cells were found to have a single point mutation G29A within the coding region of the
DPM2 gene, resulting in a glycine to glutamic acid change in amino acid residue 10 of the peptide. Moreover, mutant DPM2 cDNA expressed a drastically reduced amount of DPM2 protein and poorly corrects the Lec15.1 cell phenotype when compared with wild type CHO DPM2 cDNA (G
29 form).</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>CHO Cells</subject><subject>Cricetinae</subject><subject>Cricetulus</subject><subject>dolichol-phosphate-mannose synthase</subject><subject>Down-Regulation - physiology</subject><subject>DPM synthase</subject><subject>DPM1</subject><subject>DPM2</subject><subject>DPM2 gene</subject><subject>Expression</subject><subject>Gene Expression Regulation, Enzymologic - physiology</subject><subject>Glycosylation</subject><subject>Hamster</subject><subject>Humans</subject><subject>Lec15.1 cells</subject><subject>Mannosyltransferases - genetics</subject><subject>Mannosyltransferases - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed - genetics</subject><subject>Mutant</subject><subject>Oligosaccharides</subject><subject>Point Mutation</subject><subject>Saccharomyces cerevisiae</subject><subject>Species Specificity</subject><subject>Structure-Activity Relationship</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1LxDAQhoMo7rr6BzxITt5aJ-lXCl7Eb1jRg4K3kKRTzdJt16Rd3H9v6i54EwIDM8-8TB5CThnEDFh-sYi1dibmAEk89jK-R6YMSog4g3SfTAEgj3jJ3ifkyPsFAGNpXh6SSSgCBLApUVfU2_ajQbrqbNvT5dCr3nYtdeiHpg8jaluqwqvW6Dw2mzCpBoMVxe9VgPwIdzW9eXniI9p_Ip2jYVnMqMGm8cfkoFaNx5NdnZG3u9vX64do_nz_eH01j0wikj7KE8614FCmyARqkfK0YFmBxmQaqlpwjQVAkVZ5UqpUaSVqrAooURSJyHWRzMj5Nnfluq8BfS-X1o8XqBa7wUtWslKI4GpG-BY0rvPeYS1Xzi6V20gGchQrF3IUK0exv72Mh6WzXfqgl1j9rexMBuByC2D449qik95YbIMo69D0sursf_k_t7GIdA</recordid><startdate>20031219</startdate><enddate>20031219</enddate><creator>Pu, Lixia</creator><creator>Scocca, Jane R</creator><creator>Walker, Brian K</creator><creator>Krag, Sharon S</creator><general>Elsevier Inc</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>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>20031219</creationdate><title>A single point mutation resulting in an adversely reduced expression of DPM2 in the Lec15.1 cells</title><author>Pu, Lixia ; Scocca, Jane R ; Walker, Brian K ; Krag, Sharon S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c383t-6322b82094e18eb84247157ecc5b0df82be70074d639a4aba8fed709e87386b73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - metabolism</topic><topic>CHO Cells</topic><topic>Cricetinae</topic><topic>Cricetulus</topic><topic>dolichol-phosphate-mannose synthase</topic><topic>Down-Regulation - physiology</topic><topic>DPM synthase</topic><topic>DPM1</topic><topic>DPM2</topic><topic>DPM2 gene</topic><topic>Expression</topic><topic>Gene Expression Regulation, Enzymologic - physiology</topic><topic>Glycosylation</topic><topic>Hamster</topic><topic>Humans</topic><topic>Lec15.1 cells</topic><topic>Mannosyltransferases - genetics</topic><topic>Mannosyltransferases - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Site-Directed - genetics</topic><topic>Mutant</topic><topic>Oligosaccharides</topic><topic>Point Mutation</topic><topic>Saccharomyces cerevisiae</topic><topic>Species Specificity</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pu, Lixia</creatorcontrib><creatorcontrib>Scocca, Jane R</creatorcontrib><creatorcontrib>Walker, Brian K</creatorcontrib><creatorcontrib>Krag, Sharon 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>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pu, Lixia</au><au>Scocca, Jane R</au><au>Walker, Brian K</au><au>Krag, Sharon S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A single point mutation resulting in an adversely reduced expression of DPM2 in the Lec15.1 cells</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2003-12-19</date><risdate>2003</risdate><volume>312</volume><issue>3</issue><spage>555</spage><epage>561</epage><pages>555-561</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Mammalian dolichol–phosphate–mannose (DPM) synthase consists of three subunits, DPM1, DPM2, and DPM3. Lec15.1 Chinese hamster ovary cells are deficient in DPM synthase activity. The present paper reports that DPM1 cDNA from wild type and Lec15.1 CHO cells were found to be identical, and transfection with CHO DPM1 cDNA did not reverse the Lec15.1 phenotype. Neither did a chimeric cDNA containing the complete hamster DPM1 open reading frame fused to the
Saccharomyces cerevisiae DPM1 C-terminal transmembrane domain. In contrast, Lec15.1 cells were found to have a single point mutation G29A within the coding region of the
DPM2 gene, resulting in a glycine to glutamic acid change in amino acid residue 10 of the peptide. Moreover, mutant DPM2 cDNA expressed a drastically reduced amount of DPM2 protein and poorly corrects the Lec15.1 cell phenotype when compared with wild type CHO DPM2 cDNA (G
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| subjects | Amino Acid Sequence Animals Carrier Proteins - genetics Carrier Proteins - metabolism CHO Cells Cricetinae Cricetulus dolichol-phosphate-mannose synthase Down-Regulation - physiology DPM synthase DPM1 DPM2 DPM2 gene Expression Gene Expression Regulation, Enzymologic - physiology Glycosylation Hamster Humans Lec15.1 cells Mannosyltransferases - genetics Mannosyltransferases - metabolism Molecular Sequence Data Mutagenesis, Site-Directed - genetics Mutant Oligosaccharides Point Mutation Saccharomyces cerevisiae Species Specificity Structure-Activity Relationship |
| title | A single point mutation resulting in an adversely reduced expression of DPM2 in the Lec15.1 cells |
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