Hsp90 facilitates accurate loading of precursor piRNAs into PIWI proteins
PIWI-interacting RNAs (piRNAs) defend the genome against transposon activity in animal gonads. The Hsp90 chaperone machinery has been implicated in the piRNA pathway, but its exact role remains obscure. Here, we examined the effect of 17-N-allylamino-17-demethoxygeldanamycin (17-AAG), an Hsp90-speci...
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Veröffentlicht in: | RNA (Cambridge) 2013-07, Vol.19 (7), p.896-901 |
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creator | Izumi, Natsuko Kawaoka, Shinpei Yasuhara, Satoshi Suzuki, Yutaka Sugano, Sumio Katsuma, Susumu Tomari, Yukihide |
description | PIWI-interacting RNAs (piRNAs) defend the genome against transposon activity in animal gonads. The Hsp90 chaperone machinery has been implicated in the piRNA pathway, but its exact role remains obscure. Here, we examined the effect of 17-N-allylamino-17-demethoxygeldanamycin (17-AAG), an Hsp90-specific inhibitor, on the piRNA pathway. In the silkworm ovary-derived BmN4 cells, 17-AAG treatment reduced the level of piRNAs and PIWI proteins. In vitro, the 5'-nucleotide preference upon precursor piRNA loading was compromised by 17-AAG, whereas 3'-end trimming and 2'-O-methylation were unaffected. Our data highlight a role of Hsp90 in accurate loading of precursor piRNAs into PIWI proteins. |
doi_str_mv | 10.1261/rna.037200.112 |
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The Hsp90 chaperone machinery has been implicated in the piRNA pathway, but its exact role remains obscure. Here, we examined the effect of 17-N-allylamino-17-demethoxygeldanamycin (17-AAG), an Hsp90-specific inhibitor, on the piRNA pathway. In the silkworm ovary-derived BmN4 cells, 17-AAG treatment reduced the level of piRNAs and PIWI proteins. In vitro, the 5'-nucleotide preference upon precursor piRNA loading was compromised by 17-AAG, whereas 3'-end trimming and 2'-O-methylation were unaffected. Our data highlight a role of Hsp90 in accurate loading of precursor piRNAs into PIWI proteins.</description><identifier>ISSN: 1355-8382</identifier><identifier>EISSN: 1469-9001</identifier><identifier>DOI: 10.1261/rna.037200.112</identifier><identifier>PMID: 23681506</identifier><language>eng</language><publisher>United States: Cold Spring Harbor Laboratory Press</publisher><subject>Animals ; Argonaute Proteins - genetics ; Argonaute Proteins - metabolism ; Benzoquinones - pharmacology ; Bombyx - cytology ; Bombyx mori ; Cell Line ; Female ; Gene Expression Regulation ; HSP90 Heat-Shock Proteins - antagonists & inhibitors ; HSP90 Heat-Shock Proteins - genetics ; HSP90 Heat-Shock Proteins - metabolism ; Immunoprecipitation ; Insect Proteins - genetics ; Insect Proteins - metabolism ; Lactams, Macrocyclic - pharmacology ; Methylation ; MicroRNAs - genetics ; MicroRNAs - metabolism ; Ovary - cytology ; RNA, Small Interfering - genetics ; RNA, Small Interfering - metabolism</subject><ispartof>RNA (Cambridge), 2013-07, Vol.19 (7), p.896-901</ispartof><rights>2013; Published by Cold Spring Harbor Laboratory Press for the RNA Society 2013</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c423t-aba92b1a1c7f35667f492c2fb23a1da1dae98f0f906da7576fcbdc7d4646885d3</citedby><cites>FETCH-LOGICAL-c423t-aba92b1a1c7f35667f492c2fb23a1da1dae98f0f906da7576fcbdc7d4646885d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3683924/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3683924/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,725,778,782,883,27913,27914,53780,53782</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23681506$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Izumi, Natsuko</creatorcontrib><creatorcontrib>Kawaoka, Shinpei</creatorcontrib><creatorcontrib>Yasuhara, Satoshi</creatorcontrib><creatorcontrib>Suzuki, Yutaka</creatorcontrib><creatorcontrib>Sugano, Sumio</creatorcontrib><creatorcontrib>Katsuma, Susumu</creatorcontrib><creatorcontrib>Tomari, Yukihide</creatorcontrib><title>Hsp90 facilitates accurate loading of precursor piRNAs into PIWI proteins</title><title>RNA (Cambridge)</title><addtitle>RNA</addtitle><description>PIWI-interacting RNAs (piRNAs) defend the genome against transposon activity in animal gonads. The Hsp90 chaperone machinery has been implicated in the piRNA pathway, but its exact role remains obscure. Here, we examined the effect of 17-N-allylamino-17-demethoxygeldanamycin (17-AAG), an Hsp90-specific inhibitor, on the piRNA pathway. In the silkworm ovary-derived BmN4 cells, 17-AAG treatment reduced the level of piRNAs and PIWI proteins. In vitro, the 5'-nucleotide preference upon precursor piRNA loading was compromised by 17-AAG, whereas 3'-end trimming and 2'-O-methylation were unaffected. Our data highlight a role of Hsp90 in accurate loading of precursor piRNAs into PIWI proteins.</description><subject>Animals</subject><subject>Argonaute Proteins - genetics</subject><subject>Argonaute Proteins - metabolism</subject><subject>Benzoquinones - pharmacology</subject><subject>Bombyx - cytology</subject><subject>Bombyx mori</subject><subject>Cell Line</subject><subject>Female</subject><subject>Gene Expression Regulation</subject><subject>HSP90 Heat-Shock Proteins - antagonists & inhibitors</subject><subject>HSP90 Heat-Shock Proteins - genetics</subject><subject>HSP90 Heat-Shock Proteins - metabolism</subject><subject>Immunoprecipitation</subject><subject>Insect Proteins - genetics</subject><subject>Insect Proteins - metabolism</subject><subject>Lactams, Macrocyclic - pharmacology</subject><subject>Methylation</subject><subject>MicroRNAs - genetics</subject><subject>MicroRNAs - metabolism</subject><subject>Ovary - cytology</subject><subject>RNA, Small Interfering - genetics</subject><subject>RNA, Small Interfering - metabolism</subject><issn>1355-8382</issn><issn>1469-9001</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9LwzAUx4Mobk6vHqVHL5350aTNRRhDXWGoiOIxpGkyI11Tk1bwvzdjc-hJCOTlfb_vSx4fAM4RnCLM0JVv5RSSHMP4RvgAjFHGeMohRIexJpSmBSnwCJyE8B6bJMrHYIQJKxCFbAzKReg4TIxUtrG97HVIpFKDj1XSOFnbdpU4k3Rex2ZwPuns0_0sJLbtXfJYvpZRcr22bTgFR0Y2QZ_t7gl4ub15ni_S5cNdOZ8tU5Vh0qeykhxXSCKVG0IZy03GscKmwkSienM0Lww0HLJa5jRnRlW1yuuMZawoaE0m4Hqb2w3VWtdKt72Xjei8XUv_JZy04q_S2jexcp8i7kw4zmLA5S7Au49Bh16sbVC6aWSr3RAEyhCmjNCM_G8ljOeoKHgerdOtVXkXgtdm_yMExQaViKjEFpWIqOLAxe899vYfNuQbA-qQDw</recordid><startdate>201307</startdate><enddate>201307</enddate><creator>Izumi, Natsuko</creator><creator>Kawaoka, Shinpei</creator><creator>Yasuhara, Satoshi</creator><creator>Suzuki, Yutaka</creator><creator>Sugano, Sumio</creator><creator>Katsuma, Susumu</creator><creator>Tomari, Yukihide</creator><general>Cold Spring Harbor Laboratory 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>7X8</scope><scope>7TM</scope><scope>5PM</scope></search><sort><creationdate>201307</creationdate><title>Hsp90 facilitates accurate loading of precursor piRNAs into PIWI proteins</title><author>Izumi, Natsuko ; Kawaoka, Shinpei ; Yasuhara, Satoshi ; Suzuki, Yutaka ; Sugano, Sumio ; Katsuma, Susumu ; Tomari, Yukihide</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c423t-aba92b1a1c7f35667f492c2fb23a1da1dae98f0f906da7576fcbdc7d4646885d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Animals</topic><topic>Argonaute Proteins - genetics</topic><topic>Argonaute Proteins - metabolism</topic><topic>Benzoquinones - pharmacology</topic><topic>Bombyx - cytology</topic><topic>Bombyx mori</topic><topic>Cell Line</topic><topic>Female</topic><topic>Gene Expression Regulation</topic><topic>HSP90 Heat-Shock Proteins - antagonists & inhibitors</topic><topic>HSP90 Heat-Shock Proteins - genetics</topic><topic>HSP90 Heat-Shock Proteins - metabolism</topic><topic>Immunoprecipitation</topic><topic>Insect Proteins - genetics</topic><topic>Insect Proteins - metabolism</topic><topic>Lactams, Macrocyclic - pharmacology</topic><topic>Methylation</topic><topic>MicroRNAs - genetics</topic><topic>MicroRNAs - metabolism</topic><topic>Ovary - cytology</topic><topic>RNA, Small Interfering - genetics</topic><topic>RNA, Small Interfering - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Izumi, Natsuko</creatorcontrib><creatorcontrib>Kawaoka, Shinpei</creatorcontrib><creatorcontrib>Yasuhara, Satoshi</creatorcontrib><creatorcontrib>Suzuki, Yutaka</creatorcontrib><creatorcontrib>Sugano, Sumio</creatorcontrib><creatorcontrib>Katsuma, Susumu</creatorcontrib><creatorcontrib>Tomari, Yukihide</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Nucleic Acids Abstracts</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>Izumi, Natsuko</au><au>Kawaoka, Shinpei</au><au>Yasuhara, Satoshi</au><au>Suzuki, Yutaka</au><au>Sugano, Sumio</au><au>Katsuma, Susumu</au><au>Tomari, Yukihide</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Hsp90 facilitates accurate loading of precursor piRNAs into PIWI proteins</atitle><jtitle>RNA (Cambridge)</jtitle><addtitle>RNA</addtitle><date>2013-07</date><risdate>2013</risdate><volume>19</volume><issue>7</issue><spage>896</spage><epage>901</epage><pages>896-901</pages><issn>1355-8382</issn><eissn>1469-9001</eissn><abstract>PIWI-interacting RNAs (piRNAs) defend the genome against transposon activity in animal gonads. The Hsp90 chaperone machinery has been implicated in the piRNA pathway, but its exact role remains obscure. Here, we examined the effect of 17-N-allylamino-17-demethoxygeldanamycin (17-AAG), an Hsp90-specific inhibitor, on the piRNA pathway. In the silkworm ovary-derived BmN4 cells, 17-AAG treatment reduced the level of piRNAs and PIWI proteins. In vitro, the 5'-nucleotide preference upon precursor piRNA loading was compromised by 17-AAG, whereas 3'-end trimming and 2'-O-methylation were unaffected. Our data highlight a role of Hsp90 in accurate loading of precursor piRNAs into PIWI proteins.</abstract><cop>United States</cop><pub>Cold Spring Harbor Laboratory Press</pub><pmid>23681506</pmid><doi>10.1261/rna.037200.112</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Animals Argonaute Proteins - genetics Argonaute Proteins - metabolism Benzoquinones - pharmacology Bombyx - cytology Bombyx mori Cell Line Female Gene Expression Regulation HSP90 Heat-Shock Proteins - antagonists & inhibitors HSP90 Heat-Shock Proteins - genetics HSP90 Heat-Shock Proteins - metabolism Immunoprecipitation Insect Proteins - genetics Insect Proteins - metabolism Lactams, Macrocyclic - pharmacology Methylation MicroRNAs - genetics MicroRNAs - metabolism Ovary - cytology RNA, Small Interfering - genetics RNA, Small Interfering - metabolism |
title | Hsp90 facilitates accurate loading of precursor piRNAs into PIWI proteins |
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