Identification of a Precursor Molecule for the RNA Moiety of the Processing Enzyme RNase P
A precursor molecule for 10Sb (M1) RNA, the RNA moiety of the RNA processing enzyme ribonuclease P (EC 3.1.26.5), is accumulated transiently in an Escherichia coli strain containing a plasmid that carries the 10Sb RNA gene. The same RNA precursor molecule is accumulated, in relatively large quantiti...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1983-01, Vol.80 (14), p.4450-4454 |
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creator | Gurevitz, Michael Jain, Swatantra K. Apirion, David |
description | A precursor molecule for 10Sb (M1) RNA, the RNA moiety of the RNA processing enzyme ribonuclease P (EC 3.1.26.5), is accumulated transiently in an Escherichia coli strain containing a plasmid that carries the 10Sb RNA gene. The same RNA precursor molecule is accumulated, in relatively large quantities, in a temperature-sensitive RNase E- mutant at the nonpermissive temperature. The RNA precursor includes 10Sb RNA and an extra 3′ fragment that contains a termination stem and loop. It can be processed in vitro to a molecule the size of 10Sb RNA. None of the four endoribonucleases of E. coli--RNase III, RNase E, RNase F, or RNase P--takes part in this cleavage reaction. Therefore, we suggest that the processing of the precursor-10Sb RNA to 10Sb RNA is carried out by a thus-far unidentified endoribonuclease. The accumulation of a RNA molecule in a RNase E- mutant that does not contain a cleavage site for RNase E has been encountered previously and can be explained by assuming the existence of a RNA processing complex in the E. coli cell. |
doi_str_mv | 10.1073/pnas.80.14.4450 |
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The same RNA precursor molecule is accumulated, in relatively large quantities, in a temperature-sensitive RNase E- mutant at the nonpermissive temperature. The RNA precursor includes 10Sb RNA and an extra 3′ fragment that contains a termination stem and loop. It can be processed in vitro to a molecule the size of 10Sb RNA. None of the four endoribonucleases of E. coli--RNase III, RNase E, RNase F, or RNase P--takes part in this cleavage reaction. Therefore, we suggest that the processing of the precursor-10Sb RNA to 10Sb RNA is carried out by a thus-far unidentified endoribonuclease. The accumulation of a RNA molecule in a RNase E- mutant that does not contain a cleavage site for RNase E has been encountered previously and can be explained by assuming the existence of a RNA processing complex in the E. coli cell.</description><identifier>ISSN: 0027-8424</identifier><identifier>DOI: 10.1073/pnas.80.14.4450</identifier><language>eng</language><publisher>National Academy of Sciences of the United States of America</publisher><subject>Electrophoresis ; Enzymes ; Escherichia coli ; Gels ; Molecules ; Nucleotides ; Oligonucleotides ; Plasmids ; RNA ; RNA precursors ; Stem cells</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1983-01, Vol.80 (14), p.4450-4454</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/14045$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/14045$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,776,780,799,27901,27902,57992,58225</link.rule.ids></links><search><creatorcontrib>Gurevitz, Michael</creatorcontrib><creatorcontrib>Jain, Swatantra K.</creatorcontrib><creatorcontrib>Apirion, David</creatorcontrib><title>Identification of a Precursor Molecule for the RNA Moiety of the Processing Enzyme RNase P</title><title>Proceedings of the National Academy of Sciences - PNAS</title><description>A precursor molecule for 10Sb (M1) RNA, the RNA moiety of the RNA processing enzyme ribonuclease P (EC 3.1.26.5), is accumulated transiently in an Escherichia coli strain containing a plasmid that carries the 10Sb RNA gene. The same RNA precursor molecule is accumulated, in relatively large quantities, in a temperature-sensitive RNase E- mutant at the nonpermissive temperature. The RNA precursor includes 10Sb RNA and an extra 3′ fragment that contains a termination stem and loop. It can be processed in vitro to a molecule the size of 10Sb RNA. None of the four endoribonucleases of E. coli--RNase III, RNase E, RNase F, or RNase P--takes part in this cleavage reaction. Therefore, we suggest that the processing of the precursor-10Sb RNA to 10Sb RNA is carried out by a thus-far unidentified endoribonuclease. The accumulation of a RNA molecule in a RNase E- mutant that does not contain a cleavage site for RNase E has been encountered previously and can be explained by assuming the existence of a RNA processing complex in the E. coli cell.</description><subject>Electrophoresis</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Gels</subject><subject>Molecules</subject><subject>Nucleotides</subject><subject>Oligonucleotides</subject><subject>Plasmids</subject><subject>RNA</subject><subject>RNA precursors</subject><subject>Stem cells</subject><issn>0027-8424</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><recordid>eNotjz1PwzAURT2ARCnMSEye2FL8GbtjVRWoVKBCsLBEjvMCrtK42M4Qfj2uynTfPTp60kXohpIZJYrfH3oTZzoXMRNCkjM0IYSpQgsmLtBljDtCyFxqMkGf6wb65FpnTXK-x77FBm8D2CFEH_Cz7_LZAW5zSd-A314WGTpI41E9km3wFmJ0_Rde9b_j_uiYmPkVOm9NF-H6P6fo42H1vnwqNq-P6-ViU-wY4amQitbKCjsvW9FSxgkTuqRMEZBKWW6o0fVcQ82kAcYawSwXNZhSMN3kFYZP0d3p7yH4nwFiqvYuWug604MfYkV5WXKmZBZvT-IuJh-qQ3B7E8aKCiIk_wOoQ1wI</recordid><startdate>19830101</startdate><enddate>19830101</enddate><creator>Gurevitz, Michael</creator><creator>Jain, Swatantra K.</creator><creator>Apirion, David</creator><general>National Academy of Sciences of the United States of America</general><scope>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>19830101</creationdate><title>Identification of a Precursor Molecule for the RNA Moiety of the Processing Enzyme RNase P</title><author>Gurevitz, Michael ; Jain, Swatantra K. ; Apirion, David</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-j203t-571b7c4c96f4f123024861270e577c3a1a8b98eb25ae22d42c34bea6428d009a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>Electrophoresis</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>Gels</topic><topic>Molecules</topic><topic>Nucleotides</topic><topic>Oligonucleotides</topic><topic>Plasmids</topic><topic>RNA</topic><topic>RNA precursors</topic><topic>Stem cells</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gurevitz, Michael</creatorcontrib><creatorcontrib>Jain, Swatantra K.</creatorcontrib><creatorcontrib>Apirion, David</creatorcontrib><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>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gurevitz, Michael</au><au>Jain, Swatantra K.</au><au>Apirion, David</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of a Precursor Molecule for the RNA Moiety of the Processing Enzyme RNase P</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><date>1983-01-01</date><risdate>1983</risdate><volume>80</volume><issue>14</issue><spage>4450</spage><epage>4454</epage><pages>4450-4454</pages><issn>0027-8424</issn><abstract>A precursor molecule for 10Sb (M1) RNA, the RNA moiety of the RNA processing enzyme ribonuclease P (EC 3.1.26.5), is accumulated transiently in an Escherichia coli strain containing a plasmid that carries the 10Sb RNA gene. The same RNA precursor molecule is accumulated, in relatively large quantities, in a temperature-sensitive RNase E- mutant at the nonpermissive temperature. The RNA precursor includes 10Sb RNA and an extra 3′ fragment that contains a termination stem and loop. It can be processed in vitro to a molecule the size of 10Sb RNA. None of the four endoribonucleases of E. coli--RNase III, RNase E, RNase F, or RNase P--takes part in this cleavage reaction. Therefore, we suggest that the processing of the precursor-10Sb RNA to 10Sb RNA is carried out by a thus-far unidentified endoribonuclease. The accumulation of a RNA molecule in a RNase E- mutant that does not contain a cleavage site for RNase E has been encountered previously and can be explained by assuming the existence of a RNA processing complex in the E. coli cell.</abstract><pub>National Academy of Sciences of the United States of America</pub><doi>10.1073/pnas.80.14.4450</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Electrophoresis Enzymes Escherichia coli Gels Molecules Nucleotides Oligonucleotides Plasmids RNA RNA precursors Stem cells |
title | Identification of a Precursor Molecule for the RNA Moiety of the Processing Enzyme RNase P |
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