Cloning and Partial Characterization of the Proteasome S4 ATPase from Plasmodium falciparum
Identifieur interne : 002298 ( Istex/Corpus ); précédent : 002297; suivant : 002299Cloning and Partial Characterization of the Proteasome S4 ATPase from Plasmodium falciparum
Auteurs : Gabriela Certad ; Abrahem Abrahem ; Elias GeorgesSource :
- Experimental Parasitology [ 0014-4894 ] ; 1999.
English descriptors
- Teeft :
- Abrahem, Academic press, Amino, Amino acid residues, Amino acid sequence, Amino acids, Annual review, Antimalarial drugs, Antisense primers, Atpase, Atpase homologue, Atpase subunits, Atpases, Biological chemistry, Cdna, Cdna encoding, Cell biology, Certad, Clone, Control antibody, Control cdna, Cytotoxicity assays, Degradation, Different clones, Encoding, Entamoeba histolytica, Eukaryotic cells, Experimental medicine, Experimental parasitology, Falciparum, High sequence identity, Immunoprecipitated, Immunoprecipitation, Irrelevant antibody, Lactacystin, Mammalian cells, Mcgill university, Molecular mass, Nitrocellulose membrane, Northern blot analysis, Open reading frame, Parasite, Parasitized, Parasitized rbcs, Partial characterization, Pathway, Pfs4, Pfs4 antiserum, Pfs4 cdna, Pfs4 cdna sequence, Pfs4 gene, Pfs4 proteins, Pfs4 sequence, Plasmodial proteins, Plasmodium, Plasmodium falciparum, Polypeptide, Positive control, Primer, Protease, Proteasome, Proteasome activities, Protein degradation, Reticulocyte lysate, Room temperature, Sequence identity, Similar molar concentrations, Southern blot analysis, Specific inhibitor, Specific interactions, Substrate specificity, Subunit, Ubiquinated proteins, Unique inserts.
Abstract
Abstract: Certad, G., Abrahem, A., and Georges, E. 1999. Cloning and Partial characterization of the proteasome S4 ATPase from Plasmodium falciparum. Experimental Parasitology93, 123–131. The ATP-ubiquitin-proteasome pathway mediates the nonlysosomal degradation of cytosolic proteins in eukaryotic cells. The activities of this pathway have been shown to regulate cell growth and differentiation through modulation of regulatory proteins. The proteasome is a large complex consisting of two multisubunit structures, the 20S and 19S(PA700) or P28 complexes, that combine to form the 26S particles. In this study, we describe the cloning of a cDNA encoding the proteasome subunit 4 ATPase homologue from Plasmodium falciparum (PFS4). Analysis of the PFS4 cDNA sequence shows an open reading frame encoding a deduced protein of 455 amino acids. Moreover, comparison of PFS4 cDNA sequence to that of genomic fragments encoding PFS4 showed identical sequences with no detectable introns. Database searches revealed a high sequence identity to those of rice, yeast, mouse, Drosophila, and human S4 ATPases. However, PFS4 contains two unique inserts of nine and seven amino acid residues in the N-terminal domain. Interestingly, only the rice S4 contains the latter (seven amino acids) insert with four identical amino acids. In vitro expression of the full-length cDNA encoding the PFS4, using a transcription-translation-coupled reticulocyte lysate, shows a 50-kDa [35S]methionine-labeled protein which was immunoprecipitated with PFS4 anti-peptide antiserum. Southern blot analysis of genomic DNA digests shows a single gene copy of PFS4 in P. falciparum. Of interest was the effect of the proteasome-specific natural product, lactacystin, on the growth of the parasite, with IC50 values of 0.6–0.92 μM. The latter IC50 values of lactacystin for different clones of P. falciparum are comparable to those obtained for mammalian cell lines (0.65 μM), suggesting the presence of a conserved proteasome complex. Moreover, lactacystin was equally toxic to drug-sensitive and resistant parasites.
Url:
DOI: 10.1006/expr.1999.4442
Links to Exploration step
ISTEX:E2DD954642F2AAB755D1D53A53200E21BCA2B11ELe document en format XML
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Cloning and Partial characterization of the proteasome S4 ATPase from Plasmodium falciparum. Experimental Parasitology93, 123–131. The ATP-ubiquitin-proteasome pathway mediates the nonlysosomal degradation of cytosolic proteins in eukaryotic cells. The activities of this pathway have been shown to regulate cell growth and differentiation through modulation of regulatory proteins. The proteasome is a large complex consisting of two multisubunit structures, the 20S and 19S(PA700) or P28 complexes, that combine to form the 26S particles. In this study, we describe the cloning of a cDNA encoding the proteasome subunit 4 ATPase homologue from Plasmodium falciparum (PFS4). Analysis of the PFS4 cDNA sequence shows an open reading frame encoding a deduced protein of 455 amino acids. Moreover, comparison of PFS4 cDNA sequence to that of genomic fragments encoding PFS4 showed identical sequences with no detectable introns. Database searches revealed a high sequence identity to those of rice, yeast, mouse, Drosophila, and human S4 ATPases. However, PFS4 contains two unique inserts of nine and seven amino acid residues in the N-terminal domain. Interestingly, only the rice S4 contains the latter (seven amino acids) insert with four identical amino acids. In vitro expression of the full-length cDNA encoding the PFS4, using a transcription-translation-coupled reticulocyte lysate, shows a 50-kDa [35S]methionine-labeled protein which was immunoprecipitated with PFS4 anti-peptide antiserum. Southern blot analysis of genomic DNA digests shows a single gene copy of PFS4 in P. falciparum. Of interest was the effect of the proteasome-specific natural product, lactacystin, on the growth of the parasite, with IC50 values of 0.6–0.92 μM. The latter IC50 values of lactacystin for different clones of P. falciparum are comparable to those obtained for mammalian cell lines (0.65 μM), suggesting the presence of a conserved proteasome complex. 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Cloning and Partial characterization of the proteasome S4 ATPase from Plasmodium falciparum. Experimental Parasitology93, 123–131. The ATP-ubiquitin-proteasome pathway mediates the nonlysosomal degradation of cytosolic proteins in eukaryotic cells. The activities of this pathway have been shown to regulate cell growth and differentiation through modulation of regulatory proteins. The proteasome is a large complex consisting of two multisubunit structures, the 20S and 19S(PA700) or P28 complexes, that combine to form the 26S particles. In this study, we describe the cloning of a cDNA encoding the proteasome subunit 4 ATPase homologue from Plasmodium falciparum (PFS4). Analysis of the PFS4 cDNA sequence shows an open reading frame encoding a deduced protein of 455 amino acids. Moreover, comparison of PFS4 cDNA sequence to that of genomic fragments encoding PFS4 showed identical sequences with no detectable introns. Database searches revealed a high sequence identity to those of rice, yeast, mouse, Drosophila, and human S4 ATPases. However, PFS4 contains two unique inserts of nine and seven amino acid residues in the N-terminal domain. Interestingly, only the rice S4 contains the latter (seven amino acids) insert with four identical amino acids. In vitro expression of the full-length cDNA encoding the PFS4, using a transcription-translation-coupled reticulocyte lysate, shows a 50-kDa [35S]methionine-labeled protein which was immunoprecipitated with PFS4 anti-peptide antiserum. Southern blot analysis of genomic DNA digests shows a single gene copy of PFS4 in P. falciparum. Of interest was the effect of the proteasome-specific natural product, lactacystin, on the growth of the parasite, with IC50 values of 0.6–0.92 μM. The latter IC50 values of lactacystin for different clones of P. falciparum are comparable to those obtained for mammalian cell lines (0.65 μM), suggesting the presence of a conserved proteasome complex. 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Research</json:string><json:string>Elias Georges</json:string><json:string>C. Parasitized</json:string><json:string>P. Falciparum</json:string><json:string>A. F. Cowman</json:string><json:string>Anne de Bellevue</json:string></persName><placeName><json:string>Cytotoxicity</json:string><json:string>Australia</json:string><json:string>Ste Anne</json:string><json:string>Canada</json:string><json:string>Quebec</json:string><json:string>Goldberg</json:string></placeName><ref_url><json:string>http://www.idealibrary.com</json:string></ref_url><ref_bibl><json:string>Innis et al. 1990</json:string><json:string>Ciechanover 1994</json:string><json:string>Tanaka 1998</json:string><json:string>Walsh 1989</json:string><json:string>Richmond et al. 1997</json:string><json:string>Reits et al 1997</json:string><json:string>Cohen and Parry 1990</json:string><json:string>Rutherford and Georges 1994</json:string><json:string>Ghislain et al. 1993</json:string><json:string>Cao and Firtel 1995</json:string><json:string>Cowman and Foote 1990</json:string><json:string>Coux et al. 1996</json:string><json:string>Ciechanover and Schwartz 1998</json:string><json:string>Weber 1987</json:string><json:string>Jungmann et al. 1993</json:string><json:string>Dick et al. 1996</json:string><json:string>Higgins 1992</json:string><json:string>Dai et al. 1998</json:string><json:string>Fenteany et al. 1995</json:string><json:string>Su and Wellems 1996</json:string><json:string>Rechsteiner et al. 1993</json:string><json:string>Leyser et al. 1993</json:string><json:string>McKerrow et al. 1993</json:string><json:string>Certad et al.</json:string><json:string>Rock and York 1996</json:string><json:string>Tosh and Kilbey 1995</json:string><json:string>Hochstrasser 1996</json:string><json:string>Trager and Jensen (1978)</json:string><json:string>Pamnani et al. 1997</json:string><json:string>Klemperer et al. 1989</json:string><json:string>Laemmli, 1970</json:string><json:string>Patel and Latterich 1998</json:string><json:string>Groll et al. 1997</json:string><json:string>Francis et al. 1997</json:string><json:string>Nelbock et al. 1990</json:string><json:string>Sambrook et al., 1989</json:string><json:string>Jain et al. 1992</json:string><json:string>Olliaro et al. 1996</json:string><json:string>Wilson et al. 1989</json:string><json:string>Georges et al. 1991</json:string><json:string>Gordon et al. 1993</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-SKN1W9FR-9</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - parasitology</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - biomedical research</json:string><json:string>3 - mycology & parasitology</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Immunology and Microbiology</json:string><json:string>3 - Immunology</json:string><json:string>1 - Health Sciences</json:string><json:string>2 - Medicine</json:string><json:string>3 - General Medicine</json:string><json:string>1 - Life Sciences</json:string><json:string>2 - Immunology and Microbiology</json:string><json:string>3 - Parasitology</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences biologiques fondamentales et appliquees. psychologie</json:string><json:string>4 - protozoaires</json:string></inist></categories><publicationDate>1999</publicationDate><copyrightDate>1999</copyrightDate><doi><json:string>10.1006/expr.1999.4442</json:string></doi><id>E2DD954642F2AAB755D1D53A53200E21BCA2B11E</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-SKN1W9FR-9/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-SKN1W9FR-9/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-SKN1W9FR-9/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Cloning and Partial Characterization of the Proteasome S4 ATPase from Plasmodium falciparum</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>©1999 Academic Press</p></licence><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</p></availability><date>1999</date></publicationStmt><notesStmt><note type="research-article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</note><note type="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note><note>This work was supported by funds from the National Sciences and Engineering Research Council of Canad (NSERC) and the World Health Organization (WHO) to E.G. Research at the Institute of Parasitology is partially supported by a grant from the FCAR pour l'aide à la recherche. G. Certad is supported by funds from the Fundacion Gran Marisal de Ayucucho and Vollmer Foundation. A. Abrahem is supported by funds from the Libyan Government.</note><note type="content">Section title: Regular Article</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Cloning and Partial Characterization of the Proteasome S4 ATPase from Plasmodium falciparum</title><author xml:id="author-0000"><persName><forename type="first">Gabriela</forename><surname>Certad</surname></persName><note type="biography">Both authors contributed equally to this work.</note><affiliation>Both authors contributed equally to this work.</affiliation><affiliation>Institute of Parasitology, McGill University, Macdonald Campus, Ste-Anne de Bellevue, Quebec, Canada</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Abrahem</forename><surname>Abrahem</surname></persName><note type="biography">Both authors contributed equally to this work.</note><affiliation>Both authors contributed equally to this work.</affiliation><affiliation>Institute of Parasitology, McGill University, Macdonald Campus, Ste-Anne de Bellevue, Quebec, Canada</affiliation></author><author xml:id="author-0002"><persName><forename type="first">Elias</forename><surname>Georges</surname></persName><affiliation>Institute of Parasitology, McGill University, Macdonald Campus, Ste-Anne de Bellevue, Quebec, Canada</affiliation></author><idno type="istex">E2DD954642F2AAB755D1D53A53200E21BCA2B11E</idno><idno type="ark">ark:/67375/6H6-SKN1W9FR-9</idno><idno type="DOI">10.1006/expr.1999.4442</idno><idno type="PII">S0014-4894(99)94442-9</idno></analytic><monogr><title level="j">Experimental Parasitology</title><title level="j" type="abbrev">YEXPR</title><idno type="pISSN">0014-4894</idno><idno type="PII">S0014-4894(00)X0031-8</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1999"></date><biblScope unit="volume">93</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="123">123</biblScope><biblScope unit="page" to="131">131</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1999</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: Certad, G., Abrahem, A., and Georges, E. 1999. Cloning and Partial characterization of the proteasome S4 ATPase from Plasmodium falciparum. Experimental Parasitology93, 123–131. The ATP-ubiquitin-proteasome pathway mediates the nonlysosomal degradation of cytosolic proteins in eukaryotic cells. The activities of this pathway have been shown to regulate cell growth and differentiation through modulation of regulatory proteins. The proteasome is a large complex consisting of two multisubunit structures, the 20S and 19S(PA700) or P28 complexes, that combine to form the 26S particles. In this study, we describe the cloning of a cDNA encoding the proteasome subunit 4 ATPase homologue from Plasmodium falciparum (PFS4). Analysis of the PFS4 cDNA sequence shows an open reading frame encoding a deduced protein of 455 amino acids. Moreover, comparison of PFS4 cDNA sequence to that of genomic fragments encoding PFS4 showed identical sequences with no detectable introns. Database searches revealed a high sequence identity to those of rice, yeast, mouse, Drosophila, and human S4 ATPases. However, PFS4 contains two unique inserts of nine and seven amino acid residues in the N-terminal domain. Interestingly, only the rice S4 contains the latter (seven amino acids) insert with four identical amino acids. In vitro expression of the full-length cDNA encoding the PFS4, using a transcription-translation-coupled reticulocyte lysate, shows a 50-kDa [35S]methionine-labeled protein which was immunoprecipitated with PFS4 anti-peptide antiserum. Southern blot analysis of genomic DNA digests shows a single gene copy of PFS4 in P. falciparum. Of interest was the effect of the proteasome-specific natural product, lactacystin, on the growth of the parasite, with IC50 values of 0.6–0.92 μM. The latter IC50 values of lactacystin for different clones of P. falciparum are comparable to those obtained for mammalian cell lines (0.65 μM), suggesting the presence of a conserved proteasome complex. Moreover, lactacystin was equally toxic to drug-sensitive and resistant parasites.</p></abstract></profileDesc><revisionDesc><change when="1999">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-SKN1W9FR-9/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla" xml:lang="en"><item-info><jid>YEXPR</jid><aid>94442</aid><ce:pii>S0014-4894(99)94442-9</ce:pii><ce:doi>10.1006/expr.1999.4442</ce:doi><ce:copyright type="full-transfer" year="1999">Academic Press</ce:copyright></item-info><head><ce:article-footnote><ce:label>☆</ce:label><ce:note-para>This work was supported by funds from the National Sciences and Engineering Research Council of Canad (NSERC) and the World Health Organization (WHO) to E.G. Research at the Institute of Parasitology is partially supported by a grant from the FCAR pour l'aide à la recherche. G. Certad is supported by funds from the Fundacion Gran Marisal de Ayucucho and Vollmer Foundation. A. Abrahem is supported by funds from the Libyan Government.</ce:note-para></ce:article-footnote><ce:dochead><ce:textfn>Regular Article</ce:textfn></ce:dochead><ce:title>Cloning and Partial Characterization of the Proteasome S4 ATPase from <ce:italic>Plasmodium falciparum</ce:italic></ce:title><ce:author-group><ce:author><ce:given-name>Gabriela</ce:given-name><ce:surname>Certad</ce:surname><ce:cross-ref refid="FN1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Abrahem</ce:given-name><ce:surname>Abrahem</ce:surname><ce:cross-ref refid="FN1">1</ce:cross-ref></ce:author><ce:author><ce:given-name>Elias</ce:given-name><ce:surname>Georges</ce:surname><ce:cross-ref refid="FN2"><ce:sup>2</ce:sup></ce:cross-ref></ce:author><ce:affiliation><ce:textfn>Institute of Parasitology, McGill University, Macdonald Campus, Ste-Anne de Bellevue, Quebec, Canada</ce:textfn></ce:affiliation><ce:footnote id="FN1"><ce:label>1</ce:label><ce:note-para>Both authors contributed equally to this work.</ce:note-para></ce:footnote><ce:footnote id="FN2"><ce:label>2</ce:label><ce:note-para>To whom correspondence should be addressed at Institute of Parasitology, McGill University, 21,111 Lakeshore Road, Ste Anne de Bellevue, Quebec, Canada, H9X 3V9. Fax: 514 398-7857. E-mail: Elias_Georges@maclan.McGill.ca.</ce:note-para></ce:footnote></ce:author-group><ce:date-received day="9" month="2" year="1999"></ce:date-received><ce:date-accepted day="6" month="7" year="1999"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Certad, G., Abrahem, A., and Georges, E. 1999. Cloning and Partial characterization of the proteasome S4 ATPase from <ce:italic>Plasmodium falciparum</ce:italic>. <ce:italic>Experimental Parasitology</ce:italic><ce:bold>93,</ce:bold> 123–131. The ATP-ubiquitin-proteasome pathway mediates the nonlysosomal degradation of cytosolic proteins in eukaryotic cells. The activities of this pathway have been shown to regulate cell growth and differentiation through modulation of regulatory proteins. The proteasome is a large complex consisting of two multisubunit structures, the 20S and 19S(PA700) or P28 complexes, that combine to form the 26S particles. In this study, we describe the cloning of a cDNA encoding the proteasome subunit 4 ATPase homologue from <ce:italic>Plasmodium falciparum</ce:italic> (PFS4). Analysis of the PFS4 cDNA sequence shows an open reading frame encoding a deduced protein of 455 amino acids. Moreover, comparison of PFS4 cDNA sequence to that of genomic fragments encoding PFS4 showed identical sequences with no detectable introns. Database searches revealed a high sequence identity to those of rice, yeast, mouse, <ce:italic>Drosophila</ce:italic>, and human S4 ATPases. However, PFS4 contains two unique inserts of nine and seven amino acid residues in the N-terminal domain. Interestingly, only the rice S4 contains the latter (seven amino acids) insert with four identical amino acids. <ce:italic>In vitro</ce:italic> expression of the full-length cDNA encoding the PFS4, using a transcription-translation-coupled reticulocyte lysate, shows a 50-kDa [<ce:sup>35</ce:sup>S]methionine-labeled protein which was immunoprecipitated with PFS4 anti-peptide antiserum. Southern blot analysis of genomic DNA digests shows a single gene copy of PFS4 in <ce:italic>P. falciparum</ce:italic>. Of interest was the effect of the proteasome-specific natural product, lactacystin, on the growth of the parasite, with IC<ce:inf>50</ce:inf> values of 0.6–0.92 μM. The latter IC<ce:inf>50</ce:inf> values of lactacystin for different clones of <ce:italic>P. falciparum</ce:italic> are comparable to those obtained for mammalian cell lines (0.65 μM), suggesting the presence of a conserved proteasome complex. Moreover, lactacystin was equally toxic to drug-sensitive and resistant parasites.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Cloning and Partial Characterization of the Proteasome S4 ATPase from Plasmodium falciparum</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Cloning and Partial Characterization of the Proteasome S4 ATPase from</title></titleInfo><name type="personal"><namePart type="given">Gabriela</namePart><namePart type="family">Certad</namePart><affiliation>Institute of Parasitology, McGill University, Macdonald Campus, Ste-Anne de Bellevue, Quebec, Canada</affiliation><description>Both authors contributed equally to this work.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Abrahem</namePart><namePart type="family">Abrahem</namePart><affiliation>Institute of Parasitology, McGill University, Macdonald Campus, Ste-Anne de Bellevue, Quebec, Canada</affiliation><description>Both authors contributed equally to this work.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Elias</namePart><namePart type="family">Georges</namePart><affiliation>Institute of Parasitology, McGill University, Macdonald Campus, Ste-Anne de Bellevue, Quebec, Canada</affiliation><description>To whom correspondence should be addressed at Institute of Parasitology, McGill University, 21,111 Lakeshore Road, Ste Anne de Bellevue, Quebec, Canada, H9X 3V9. Fax: 514 398-7857. E-mail: Elias_Georges@maclan.McGill.ca.</description><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1999</dateIssued><copyrightDate encoding="w3cdtf">1999</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: Certad, G., Abrahem, A., and Georges, E. 1999. Cloning and Partial characterization of the proteasome S4 ATPase from Plasmodium falciparum. Experimental Parasitology93, 123–131. The ATP-ubiquitin-proteasome pathway mediates the nonlysosomal degradation of cytosolic proteins in eukaryotic cells. The activities of this pathway have been shown to regulate cell growth and differentiation through modulation of regulatory proteins. The proteasome is a large complex consisting of two multisubunit structures, the 20S and 19S(PA700) or P28 complexes, that combine to form the 26S particles. In this study, we describe the cloning of a cDNA encoding the proteasome subunit 4 ATPase homologue from Plasmodium falciparum (PFS4). Analysis of the PFS4 cDNA sequence shows an open reading frame encoding a deduced protein of 455 amino acids. Moreover, comparison of PFS4 cDNA sequence to that of genomic fragments encoding PFS4 showed identical sequences with no detectable introns. Database searches revealed a high sequence identity to those of rice, yeast, mouse, Drosophila, and human S4 ATPases. However, PFS4 contains two unique inserts of nine and seven amino acid residues in the N-terminal domain. Interestingly, only the rice S4 contains the latter (seven amino acids) insert with four identical amino acids. In vitro expression of the full-length cDNA encoding the PFS4, using a transcription-translation-coupled reticulocyte lysate, shows a 50-kDa [35S]methionine-labeled protein which was immunoprecipitated with PFS4 anti-peptide antiserum. Southern blot analysis of genomic DNA digests shows a single gene copy of PFS4 in P. falciparum. Of interest was the effect of the proteasome-specific natural product, lactacystin, on the growth of the parasite, with IC50 values of 0.6–0.92 μM. The latter IC50 values of lactacystin for different clones of P. falciparum are comparable to those obtained for mammalian cell lines (0.65 μM), suggesting the presence of a conserved proteasome complex. Moreover, lactacystin was equally toxic to drug-sensitive and resistant parasites.</abstract><note>This work was supported by funds from the National Sciences and Engineering Research Council of Canad (NSERC) and the World Health Organization (WHO) to E.G. Research at the Institute of Parasitology is partially supported by a grant from the FCAR pour l'aide à la recherche. G. Certad is supported by funds from the Fundacion Gran Marisal de Ayucucho and Vollmer Foundation. A. Abrahem is supported by funds from the Libyan Government.</note><note type="content">Section title: Regular Article</note><relatedItem type="host"><titleInfo><title>Experimental Parasitology</title></titleInfo><titleInfo type="abbreviated"><title>YEXPR</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1999</dateIssued></originInfo><identifier type="ISSN">0014-4894</identifier><identifier type="PII">S0014-4894(00)X0031-8</identifier><part><date>1999</date><detail type="volume"><number>93</number><caption>vol.</caption></detail><detail type="issue"><number>3</number><caption>no.</caption></detail><extent unit="issue-pages"><start>123</start><end>180</end></extent><extent unit="pages"><start>123</start><end>131</end></extent></part></relatedItem><identifier type="istex">E2DD954642F2AAB755D1D53A53200E21BCA2B11E</identifier><identifier type="ark">ark:/67375/6H6-SKN1W9FR-9</identifier><identifier type="DOI">10.1006/expr.1999.4442</identifier><identifier type="PII">S0014-4894(99)94442-9</identifier><accessCondition type="use and reproduction" contentType="copyright">©1999 Academic Press</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource><recordOrigin>Academic Press, ©1999</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-SKN1W9FR-9/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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