Peroxisome-deficient Chinese hamster ovary cells with point mutations in peroxisome assembly factor-1
Chinese hamster ovary (CHO) mutant cells deficient in peroxisome biogenesis regain peroxisomes after transfection with a cDNA coding for peroxisome assembly factor (PAF)-1 from rat liver. Reconstitution of the transfected mutant cells with wild-type cytoplasm was not required, demonstrating that exp...
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| Veröffentlicht in: | The Journal of biological chemistry 1993-06, Vol.268 (17), p.12631-12636 |
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| container_title | The Journal of biological chemistry |
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| creator | THIERINGER, R RAETZ, C. R. H |
| description | Chinese hamster ovary (CHO) mutant cells deficient in peroxisome biogenesis regain peroxisomes after transfection with a cDNA
coding for peroxisome assembly factor (PAF)-1 from rat liver. Reconstitution of the transfected mutant cells with wild-type
cytoplasm was not required, demonstrating that expression of the PAF-1 gene alone was sufficient for the restoration of peroxisome
biogenesis. Plasmalogen biosynthesis in the transfected mutants was also restored to approximately wild-type levels. The nucleotide
sequence of the cDNA encoding the open reading frame for PAF-1 from CHO-K1 cells was determined. This allowed us to identify
point mutations of PAF-1 in two peroxisomal mutant cell lines. The mutation in ZR-78 cells changed a cysteine to a tyrosine
codon in a region located at the carboxyl terminus of the protein, which resembles the zinc finger motif of DNA-binding proteins.
A point mutation in the PAF-1 gene of ZR-82 leads to premature termination. |
| doi_str_mv | 10.1016/S0021-9258(18)31435-2 |
| format | Article |
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coding for peroxisome assembly factor (PAF)-1 from rat liver. Reconstitution of the transfected mutant cells with wild-type
cytoplasm was not required, demonstrating that expression of the PAF-1 gene alone was sufficient for the restoration of peroxisome
biogenesis. Plasmalogen biosynthesis in the transfected mutants was also restored to approximately wild-type levels. The nucleotide
sequence of the cDNA encoding the open reading frame for PAF-1 from CHO-K1 cells was determined. This allowed us to identify
point mutations of PAF-1 in two peroxisomal mutant cell lines. The mutation in ZR-78 cells changed a cysteine to a tyrosine
codon in a region located at the carboxyl terminus of the protein, which resembles the zinc finger motif of DNA-binding proteins.
A point mutation in the PAF-1 gene of ZR-82 leads to premature termination.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)31435-2</identifier><identifier>PMID: 7685346</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Biological and medical sciences ; Catalase - analysis ; Catalase - metabolism ; cDNA ; Cell Membrane - metabolism ; Cell structures and functions ; CHO Cells ; Cloning, Molecular ; Codon - genetics ; Cricetinae ; DNA ; DNA Mutational Analysis ; Fundamental and applied biological sciences. Psychology ; genes ; Humans ; Liver - metabolism ; Lysosome, phagosome ; Membrane Proteins - biosynthesis ; Membrane Proteins - genetics ; Microbodies - metabolism ; Molecular and cellular biology ; Molecular Sequence Data ; Mutagenesis ; nucleotide sequence ; Peroxisomal Biogenesis Factor 2 ; peroxisome assembly factor-1 ; plasmalogen ; Point Mutation ; Poly A - isolation & purification ; Poly A - metabolism ; predictions ; Rats ; RNA - isolation & purification ; RNA - metabolism ; RNA, Messenger - isolation & purification ; RNA, Messenger - metabolism ; Sequence Homology, Amino Acid ; synthesis ; Tyrosine</subject><ispartof>The Journal of biological chemistry, 1993-06, Vol.268 (17), p.12631-12636</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3552-c6ee2539be852734b443f2dd2805c5fc58746ec91783ae9b3e7dcce3ad381e853</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4820584$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7685346$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>THIERINGER, R</creatorcontrib><creatorcontrib>RAETZ, C. R. H</creatorcontrib><title>Peroxisome-deficient Chinese hamster ovary cells with point mutations in peroxisome assembly factor-1</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Chinese hamster ovary (CHO) mutant cells deficient in peroxisome biogenesis regain peroxisomes after transfection with a cDNA
coding for peroxisome assembly factor (PAF)-1 from rat liver. Reconstitution of the transfected mutant cells with wild-type
cytoplasm was not required, demonstrating that expression of the PAF-1 gene alone was sufficient for the restoration of peroxisome
biogenesis. Plasmalogen biosynthesis in the transfected mutants was also restored to approximately wild-type levels. The nucleotide
sequence of the cDNA encoding the open reading frame for PAF-1 from CHO-K1 cells was determined. This allowed us to identify
point mutations of PAF-1 in two peroxisomal mutant cell lines. The mutation in ZR-78 cells changed a cysteine to a tyrosine
codon in a region located at the carboxyl terminus of the protein, which resembles the zinc finger motif of DNA-binding proteins.
A point mutation in the PAF-1 gene of ZR-82 leads to premature termination.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Catalase - analysis</subject><subject>Catalase - metabolism</subject><subject>cDNA</subject><subject>Cell Membrane - metabolism</subject><subject>Cell structures and functions</subject><subject>CHO Cells</subject><subject>Cloning, Molecular</subject><subject>Codon - genetics</subject><subject>Cricetinae</subject><subject>DNA</subject><subject>DNA Mutational Analysis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>genes</subject><subject>Humans</subject><subject>Liver - metabolism</subject><subject>Lysosome, phagosome</subject><subject>Membrane Proteins - biosynthesis</subject><subject>Membrane Proteins - genetics</subject><subject>Microbodies - metabolism</subject><subject>Molecular and cellular biology</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis</subject><subject>nucleotide sequence</subject><subject>Peroxisomal Biogenesis Factor 2</subject><subject>peroxisome assembly factor-1</subject><subject>plasmalogen</subject><subject>Point Mutation</subject><subject>Poly A - isolation & purification</subject><subject>Poly A - metabolism</subject><subject>predictions</subject><subject>Rats</subject><subject>RNA - isolation & purification</subject><subject>RNA - metabolism</subject><subject>RNA, Messenger - isolation & purification</subject><subject>RNA, Messenger - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>synthesis</subject><subject>Tyrosine</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkE1v1DAQhi0EKkvLT6jkA0JwSOvxR-Ic0YoWpEqtVJB6sxxn0rhK4sWTpfTfN9uulrnMYZ53xn4YOwVxBgLK81shJBS1NPYL2K8KtDKFfMNWIKwqlIG7t2x1QN6zD0QPYildwxE7qkprlC5XDG8wp3-R0ohFi10MEaeZr_s4ISHv_UgzZp7--vzEAw4D8cc493yT4oKN29nPMU3E48Q3h0XcE-HYDE-882FOuYAT9q7zA-HHfT9mvy--_1r_KK6uL3-uv10VQRkji1AiSqPqBq2RldKN1qqTbSutMMF0wdhKlxhqqKzyWDcKqzYEVL5VFpaMOmafX_ducvqzRZrdGGn3bD9h2pKD0kgLRi6geQVDTkQZO7fJcVw-6UC4nV73otft3Dmw7kWv2-VO9we2zYjtIbX3ucw_7eeegh-67KcQ6YBpK4Wx-j_Wx_v-MWZ0TUyhx9HJcrlXOZClAvUMr3qP0Q</recordid><startdate>19930615</startdate><enddate>19930615</enddate><creator>THIERINGER, R</creator><creator>RAETZ, C. R. H</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>IQODW</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>7QL</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>19930615</creationdate><title>Peroxisome-deficient Chinese hamster ovary cells with point mutations in peroxisome assembly factor-1</title><author>THIERINGER, R ; RAETZ, C. R. H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3552-c6ee2539be852734b443f2dd2805c5fc58746ec91783ae9b3e7dcce3ad381e853</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Catalase - analysis</topic><topic>Catalase - metabolism</topic><topic>cDNA</topic><topic>Cell Membrane - metabolism</topic><topic>Cell structures and functions</topic><topic>CHO Cells</topic><topic>Cloning, Molecular</topic><topic>Codon - genetics</topic><topic>Cricetinae</topic><topic>DNA</topic><topic>DNA Mutational Analysis</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>genes</topic><topic>Humans</topic><topic>Liver - metabolism</topic><topic>Lysosome, phagosome</topic><topic>Membrane Proteins - biosynthesis</topic><topic>Membrane Proteins - genetics</topic><topic>Microbodies - metabolism</topic><topic>Molecular and cellular biology</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis</topic><topic>nucleotide sequence</topic><topic>Peroxisomal Biogenesis Factor 2</topic><topic>peroxisome assembly factor-1</topic><topic>plasmalogen</topic><topic>Point Mutation</topic><topic>Poly A - isolation & purification</topic><topic>Poly A - metabolism</topic><topic>predictions</topic><topic>Rats</topic><topic>RNA - isolation & purification</topic><topic>RNA - metabolism</topic><topic>RNA, Messenger - isolation & purification</topic><topic>RNA, Messenger - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>synthesis</topic><topic>Tyrosine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>THIERINGER, R</creatorcontrib><creatorcontrib>RAETZ, C. R. H</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>THIERINGER, R</au><au>RAETZ, C. R. H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Peroxisome-deficient Chinese hamster ovary cells with point mutations in peroxisome assembly factor-1</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1993-06-15</date><risdate>1993</risdate><volume>268</volume><issue>17</issue><spage>12631</spage><epage>12636</epage><pages>12631-12636</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Chinese hamster ovary (CHO) mutant cells deficient in peroxisome biogenesis regain peroxisomes after transfection with a cDNA
coding for peroxisome assembly factor (PAF)-1 from rat liver. Reconstitution of the transfected mutant cells with wild-type
cytoplasm was not required, demonstrating that expression of the PAF-1 gene alone was sufficient for the restoration of peroxisome
biogenesis. Plasmalogen biosynthesis in the transfected mutants was also restored to approximately wild-type levels. The nucleotide
sequence of the cDNA encoding the open reading frame for PAF-1 from CHO-K1 cells was determined. This allowed us to identify
point mutations of PAF-1 in two peroxisomal mutant cell lines. The mutation in ZR-78 cells changed a cysteine to a tyrosine
codon in a region located at the carboxyl terminus of the protein, which resembles the zinc finger motif of DNA-binding proteins.
A point mutation in the PAF-1 gene of ZR-82 leads to premature termination.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>7685346</pmid><doi>10.1016/S0021-9258(18)31435-2</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Base Sequence Biological and medical sciences Catalase - analysis Catalase - metabolism cDNA Cell Membrane - metabolism Cell structures and functions CHO Cells Cloning, Molecular Codon - genetics Cricetinae DNA DNA Mutational Analysis Fundamental and applied biological sciences. Psychology genes Humans Liver - metabolism Lysosome, phagosome Membrane Proteins - biosynthesis Membrane Proteins - genetics Microbodies - metabolism Molecular and cellular biology Molecular Sequence Data Mutagenesis nucleotide sequence Peroxisomal Biogenesis Factor 2 peroxisome assembly factor-1 plasmalogen Point Mutation Poly A - isolation & purification Poly A - metabolism predictions Rats RNA - isolation & purification RNA - metabolism RNA, Messenger - isolation & purification RNA, Messenger - metabolism Sequence Homology, Amino Acid synthesis Tyrosine |
| title | Peroxisome-deficient Chinese hamster ovary cells with point mutations in peroxisome assembly factor-1 |
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