Rpp14 and Rpp29, two protein subunits of human ribonuclease P
In HeLa cells, the tRNA processing enzyme ribonuclease P (RNase P) consists of an RNA molecule associated with at least eight protein subunits, hPop1, Rpp14, Rpp20, Rpp25, Rpp29, Rpp30, Rpp38, and Rpp40. Five of these proteins (hPop1p, Rpp20, Rpp30, Rpp38, and Rpp40) have been partially characterize...
Gespeichert in:
| Veröffentlicht in: | RNA (Cambridge) 1999-02, Vol.5 (2), p.153-157, Article S135583829800185X |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 157 |
|---|---|
| container_issue | 2 |
| container_start_page | 153 |
| container_title | RNA (Cambridge) |
| container_volume | 5 |
| creator | JARROUS, NAYEF EDER, PAUL S. WESOLOWSKI, DONNA ALTMAN, SIDNEY |
| description | In HeLa cells, the tRNA processing enzyme ribonuclease
P (RNase P) consists of an RNA molecule associated with
at least eight protein subunits, hPop1, Rpp14, Rpp20, Rpp25,
Rpp29, Rpp30, Rpp38, and Rpp40. Five of these proteins
(hPop1p, Rpp20, Rpp30, Rpp38, and Rpp40) have been partially
characterized. Here we report on the cDNA cloning and immunobiochemical
analysis of Rpp14 and Rpp29. Polyclonal rabbit antibodies
raised against recombinant Rpp14 and Rpp29 recognize their
corresponding antigens in HeLa cells and precipitate catalytically
active RNase P. Rpp29 shows 23% identity with Pop4p, a
subunit of yeast nuclear RNase P and the ribosomal RNA
processing enzyme RNase MRP. Rpp14, by contrast, exhibits
no significant homology to any known yeast gene. Thus,
human RNase P differs in the details of its protein composition,
and perhaps in the functions of some of these proteins,
from the yeast enzyme. |
| doi_str_mv | 10.1017/S135583829800185X |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1369747</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><cupid>10_1017_S135583829800185X</cupid><sourcerecordid>17254400</sourcerecordid><originalsourceid>FETCH-LOGICAL-c470t-819f723cb890e4b57261142e71c3a9ff9a245218e16bec6fea478d16240cc0193</originalsourceid><addsrcrecordid>eNqFkUtr3DAUhUVpyOTRH9BN0aqrOtWVZT0WDZSheUAgIQ_oTsgaOeNgS45ktfTfV8MMIaXQrnSlc-6H7j0IvQdyAgTE5zuom0bWkipJCMjm-xt0AIyrSpXr21IXudroC3SY0lN5rIu8jxZACGXAxQH6cjtNwLDxK1wqqj7h-WfAUwyz6z1Ouc2-nxMOHV7n0Xgc-zb4bAdnksM3x2ivM0Ny73bnEXo4-3a_vKiurs8vl1-vKssEmSsJqhO0tq1UxLG2EZQDMOoE2NqorlOGsoaCdMBbZ3nnDBNyBZwyYi0BVR-h0y13yu3oVtb5OZpBT7EfTfylg-n1n4rv1_ox_NBQcyWYKICPO0AMz9mlWY99sm4YjHchJ81VIynh8r9GELRhjJBihK3RxpBSdN3Lb4DoTTr6r3RKz4fXY7zq2MZRDPUOasY29qtHp59Cjr7s9h_Y3-tLmKw</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>17254400</pqid></control><display><type>article</type><title>Rpp14 and Rpp29, two protein subunits of human ribonuclease P</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><creator>JARROUS, NAYEF ; EDER, PAUL S. ; WESOLOWSKI, DONNA ; ALTMAN, SIDNEY</creator><creatorcontrib>JARROUS, NAYEF ; EDER, PAUL S. ; WESOLOWSKI, DONNA ; ALTMAN, SIDNEY</creatorcontrib><description>In HeLa cells, the tRNA processing enzyme ribonuclease
P (RNase P) consists of an RNA molecule associated with
at least eight protein subunits, hPop1, Rpp14, Rpp20, Rpp25,
Rpp29, Rpp30, Rpp38, and Rpp40. Five of these proteins
(hPop1p, Rpp20, Rpp30, Rpp38, and Rpp40) have been partially
characterized. Here we report on the cDNA cloning and immunobiochemical
analysis of Rpp14 and Rpp29. Polyclonal rabbit antibodies
raised against recombinant Rpp14 and Rpp29 recognize their
corresponding antigens in HeLa cells and precipitate catalytically
active RNase P. Rpp29 shows 23% identity with Pop4p, a
subunit of yeast nuclear RNase P and the ribosomal RNA
processing enzyme RNase MRP. Rpp14, by contrast, exhibits
no significant homology to any known yeast gene. Thus,
human RNase P differs in the details of its protein composition,
and perhaps in the functions of some of these proteins,
from the yeast enzyme.</description><identifier>ISSN: 1355-8382</identifier><identifier>EISSN: 1469-9001</identifier><identifier>DOI: 10.1017/S135583829800185X</identifier><identifier>PMID: 10024167</identifier><language>eng</language><publisher>United States: Cambridge University Press</publisher><subject>Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Endoribonucleases - genetics ; Fungal Proteins - genetics ; Genes, Fungal - genetics ; HeLa Cells - enzymology ; Humans ; Molecular Sequence Data ; Precipitin Tests ; Recombinant Proteins - genetics ; Ribonuclease P ; Ribonucleoproteins - genetics ; RNA, Catalytic - genetics ; Sequence Alignment</subject><ispartof>RNA (Cambridge), 1999-02, Vol.5 (2), p.153-157, Article S135583829800185X</ispartof><rights>1999 RNA Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c470t-819f723cb890e4b57261142e71c3a9ff9a245218e16bec6fea478d16240cc0193</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1369747/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1369747/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27903,27904,53769,53771</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10024167$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>JARROUS, NAYEF</creatorcontrib><creatorcontrib>EDER, PAUL S.</creatorcontrib><creatorcontrib>WESOLOWSKI, DONNA</creatorcontrib><creatorcontrib>ALTMAN, SIDNEY</creatorcontrib><title>Rpp14 and Rpp29, two protein subunits of human ribonuclease P</title><title>RNA (Cambridge)</title><addtitle>RNA</addtitle><description>In HeLa cells, the tRNA processing enzyme ribonuclease
P (RNase P) consists of an RNA molecule associated with
at least eight protein subunits, hPop1, Rpp14, Rpp20, Rpp25,
Rpp29, Rpp30, Rpp38, and Rpp40. Five of these proteins
(hPop1p, Rpp20, Rpp30, Rpp38, and Rpp40) have been partially
characterized. Here we report on the cDNA cloning and immunobiochemical
analysis of Rpp14 and Rpp29. Polyclonal rabbit antibodies
raised against recombinant Rpp14 and Rpp29 recognize their
corresponding antigens in HeLa cells and precipitate catalytically
active RNase P. Rpp29 shows 23% identity with Pop4p, a
subunit of yeast nuclear RNase P and the ribosomal RNA
processing enzyme RNase MRP. Rpp14, by contrast, exhibits
no significant homology to any known yeast gene. Thus,
human RNase P differs in the details of its protein composition,
and perhaps in the functions of some of these proteins,
from the yeast enzyme.</description><subject>Amino Acid Sequence</subject><subject>Base Sequence</subject><subject>Cloning, Molecular</subject><subject>Endoribonucleases - genetics</subject><subject>Fungal Proteins - genetics</subject><subject>Genes, Fungal - genetics</subject><subject>HeLa Cells - enzymology</subject><subject>Humans</subject><subject>Molecular Sequence Data</subject><subject>Precipitin Tests</subject><subject>Recombinant Proteins - genetics</subject><subject>Ribonuclease P</subject><subject>Ribonucleoproteins - genetics</subject><subject>RNA, Catalytic - genetics</subject><subject>Sequence Alignment</subject><issn>1355-8382</issn><issn>1469-9001</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtr3DAUhUVpyOTRH9BN0aqrOtWVZT0WDZSheUAgIQ_oTsgaOeNgS45ktfTfV8MMIaXQrnSlc-6H7j0IvQdyAgTE5zuom0bWkipJCMjm-xt0AIyrSpXr21IXudroC3SY0lN5rIu8jxZACGXAxQH6cjtNwLDxK1wqqj7h-WfAUwyz6z1Ouc2-nxMOHV7n0Xgc-zb4bAdnksM3x2ivM0Ny73bnEXo4-3a_vKiurs8vl1-vKssEmSsJqhO0tq1UxLG2EZQDMOoE2NqorlOGsoaCdMBbZ3nnDBNyBZwyYi0BVR-h0y13yu3oVtb5OZpBT7EfTfylg-n1n4rv1_ox_NBQcyWYKICPO0AMz9mlWY99sm4YjHchJ81VIynh8r9GELRhjJBihK3RxpBSdN3Lb4DoTTr6r3RKz4fXY7zq2MZRDPUOasY29qtHp59Cjr7s9h_Y3-tLmKw</recordid><startdate>199902</startdate><enddate>199902</enddate><creator>JARROUS, NAYEF</creator><creator>EDER, PAUL S.</creator><creator>WESOLOWSKI, DONNA</creator><creator>ALTMAN, SIDNEY</creator><general>Cambridge University Press</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>7X8</scope><scope>5PM</scope></search><sort><creationdate>199902</creationdate><title>Rpp14 and Rpp29, two protein subunits of human ribonuclease P</title><author>JARROUS, NAYEF ; EDER, PAUL S. ; WESOLOWSKI, DONNA ; ALTMAN, SIDNEY</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c470t-819f723cb890e4b57261142e71c3a9ff9a245218e16bec6fea478d16240cc0193</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Amino Acid Sequence</topic><topic>Base Sequence</topic><topic>Cloning, Molecular</topic><topic>Endoribonucleases - genetics</topic><topic>Fungal Proteins - genetics</topic><topic>Genes, Fungal - genetics</topic><topic>HeLa Cells - enzymology</topic><topic>Humans</topic><topic>Molecular Sequence Data</topic><topic>Precipitin Tests</topic><topic>Recombinant Proteins - genetics</topic><topic>Ribonuclease P</topic><topic>Ribonucleoproteins - genetics</topic><topic>RNA, Catalytic - genetics</topic><topic>Sequence Alignment</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>JARROUS, NAYEF</creatorcontrib><creatorcontrib>EDER, PAUL S.</creatorcontrib><creatorcontrib>WESOLOWSKI, DONNA</creatorcontrib><creatorcontrib>ALTMAN, SIDNEY</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>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>RNA (Cambridge)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>JARROUS, NAYEF</au><au>EDER, PAUL S.</au><au>WESOLOWSKI, DONNA</au><au>ALTMAN, SIDNEY</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Rpp14 and Rpp29, two protein subunits of human ribonuclease P</atitle><jtitle>RNA (Cambridge)</jtitle><addtitle>RNA</addtitle><date>1999-02</date><risdate>1999</risdate><volume>5</volume><issue>2</issue><spage>153</spage><epage>157</epage><pages>153-157</pages><artnum>S135583829800185X</artnum><issn>1355-8382</issn><eissn>1469-9001</eissn><abstract>In HeLa cells, the tRNA processing enzyme ribonuclease
P (RNase P) consists of an RNA molecule associated with
at least eight protein subunits, hPop1, Rpp14, Rpp20, Rpp25,
Rpp29, Rpp30, Rpp38, and Rpp40. Five of these proteins
(hPop1p, Rpp20, Rpp30, Rpp38, and Rpp40) have been partially
characterized. Here we report on the cDNA cloning and immunobiochemical
analysis of Rpp14 and Rpp29. Polyclonal rabbit antibodies
raised against recombinant Rpp14 and Rpp29 recognize their
corresponding antigens in HeLa cells and precipitate catalytically
active RNase P. Rpp29 shows 23% identity with Pop4p, a
subunit of yeast nuclear RNase P and the ribosomal RNA
processing enzyme RNase MRP. Rpp14, by contrast, exhibits
no significant homology to any known yeast gene. Thus,
human RNase P differs in the details of its protein composition,
and perhaps in the functions of some of these proteins,
from the yeast enzyme.</abstract><cop>United States</cop><pub>Cambridge University Press</pub><pmid>10024167</pmid><doi>10.1017/S135583829800185X</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1355-8382 |
| ispartof | RNA (Cambridge), 1999-02, Vol.5 (2), p.153-157, Article S135583829800185X |
| issn | 1355-8382 1469-9001 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1369747 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Base Sequence Cloning, Molecular Endoribonucleases - genetics Fungal Proteins - genetics Genes, Fungal - genetics HeLa Cells - enzymology Humans Molecular Sequence Data Precipitin Tests Recombinant Proteins - genetics Ribonuclease P Ribonucleoproteins - genetics RNA, Catalytic - genetics Sequence Alignment |
| title | Rpp14 and Rpp29, two protein subunits of human ribonuclease P |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-25T23%3A37%3A53IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Rpp14%20and%20Rpp29,%20two%20protein%20subunits%20of%20human%20ribonuclease%20P&rft.jtitle=RNA%20(Cambridge)&rft.au=JARROUS,%20NAYEF&rft.date=1999-02&rft.volume=5&rft.issue=2&rft.spage=153&rft.epage=157&rft.pages=153-157&rft.artnum=S135583829800185X&rft.issn=1355-8382&rft.eissn=1469-9001&rft_id=info:doi/10.1017/S135583829800185X&rft_dat=%3Cproquest_pubme%3E17254400%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=17254400&rft_id=info:pmid/10024167&rft_cupid=10_1017_S135583829800185X&rfr_iscdi=true |