Recognition of tRNA His in an RNase P-Free Nanoarchaeum
The 5' extra guanosine with 5'-monophosphate at position -1 (G-1) of tRNA (p-tRNA ) is a nearly universal feature that establishes tRNA identity. G-1 is either genome encoded and retained after processing by RNase P (RNase P) or posttranscriptionally incorporated by tRNA guanylyltransferas...
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| creator | Ivanesthi, Indira Rizqita Rida, Gita Riswana Nawung Setiawibawa, Aditya Aryandi Tseng, Yi-Kuan Muammar, Arief Wang, Chien-Chia |
| description | The 5' extra guanosine with 5'-monophosphate at position -1 (G-1) of tRNA
(p-tRNA
) is a nearly universal feature that establishes tRNA
identity. G-1 is either genome encoded and retained after processing by RNase P (RNase P) or posttranscriptionally incorporated by tRNA
guanylyltransferase (Thg1) after RNase P cleavage. However, RNase P is not found in the hyperthermophilic archaeum Nanoarchaeum equitans; instead, all of its tRNAs, including tRNA
, are transcribed as leaderless tRNAs with 5'-triphosphate (ppp-tRNAs). How N. equitans histidyl-tRNA synthetase (NeHisRS) recognizes its cognate tRNA (NetRNA
) is of particular interest. In this paper, we show that G-1 serves as the major identity element of NetRNA
, with its anticodon performing a similar role, though to a lesser extent. Moreover, NeHisRS distinctly preferred p-tRNA
over ppp-tRNA
(~5-fold difference). Unlike other prokaryotic HisRSs, which strongly prefer tRNA
with C73, this enzyme could charge tRNAs
with A73 and C73 with nearly equal efficiency. As a result, mutation at the C73-recognition amino acid residue Q112 had only a minor effect ( |
| doi_str_mv | 10.1128/spectrum.04621-22 |
| format | Article |
| fullrecord | <record><control><sourceid>pubmed_cross</sourceid><recordid>TN_cdi_crossref_primary_10_1128_spectrum_04621_22</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>36840576</sourcerecordid><originalsourceid>FETCH-LOGICAL-c1562-443de2f9beb26e9e3e3ae0c91d369e9ac5f3d19eb14375caf13f7ed85ce580313</originalsourceid><addsrcrecordid>eNpNkMtOwzAURC0EolXpB7BB_gEXXzt24mVVUYpUBRTBOnKcawgiD9nJgr8HWopYzWzOSHMIuQa-AhDZbRzQjWFqVzzRApgQZ2QuQCvGE5Oe_-szsozxnXMOwJVQ4pLMpM4SrlI9J2mBrn_tmrHpO9p7Ohb5mu6aSJuO2o4WuY1In9g2INLcdr0N7s3i1F6RC28_Ii5_c0FetnfPmx3bP94_bNZ75kBpwZJE1ii8qbASGg1KlBa5M1BLbdBYp7yswWAFiUyVsx6kT7HOlEOVcQlyQeC460IfY0BfDqFpbfgsgZc_HsqTh_LgoRTim7k5MsNUtVj_EafX8guTAFmx</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Recognition of tRNA His in an RNase P-Free Nanoarchaeum</title><source>DOAJ Directory of Open Access Journals</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>PubMed Central</source><creator>Ivanesthi, Indira Rizqita ; Rida, Gita Riswana Nawung ; Setiawibawa, Aditya Aryandi ; Tseng, Yi-Kuan ; Muammar, Arief ; Wang, Chien-Chia</creator><contributor>Frances Yap, M.-N.</contributor><creatorcontrib>Ivanesthi, Indira Rizqita ; Rida, Gita Riswana Nawung ; Setiawibawa, Aditya Aryandi ; Tseng, Yi-Kuan ; Muammar, Arief ; Wang, Chien-Chia ; Frances Yap, M.-N.</creatorcontrib><description>The 5' extra guanosine with 5'-monophosphate at position -1 (G-1) of tRNA
(p-tRNA
) is a nearly universal feature that establishes tRNA
identity. G-1 is either genome encoded and retained after processing by RNase P (RNase P) or posttranscriptionally incorporated by tRNA
guanylyltransferase (Thg1) after RNase P cleavage. However, RNase P is not found in the hyperthermophilic archaeum Nanoarchaeum equitans; instead, all of its tRNAs, including tRNA
, are transcribed as leaderless tRNAs with 5'-triphosphate (ppp-tRNAs). How N. equitans histidyl-tRNA synthetase (NeHisRS) recognizes its cognate tRNA (NetRNA
) is of particular interest. In this paper, we show that G-1 serves as the major identity element of NetRNA
, with its anticodon performing a similar role, though to a lesser extent. Moreover, NeHisRS distinctly preferred p-tRNA
over ppp-tRNA
(~5-fold difference). Unlike other prokaryotic HisRSs, which strongly prefer tRNA
with C73, this enzyme could charge tRNAs
with A73 and C73 with nearly equal efficiency. As a result, mutation at the C73-recognition amino acid residue Q112 had only a minor effect (<2-fold reduction). This study suggests that NeHisRS has evolved to disregard C73, but it still maintains its evolutionarily preserved preference toward tRNA
with 5'-monophosphate.
Mature tRNA
has, at its 5'-terminus, an extra guanosine with 5'-monophosphate, designated G-1. G-1 is the major recognition element for histidyl-tRNA synthetase (HisRS), regardless of whether it is of eukaryotic or prokaryotic origin. However, in the hyperthermophilic archaeum Nanoarchaeum equitans, all its tRNAs, including tRNA
, are transcribed as leaderless tRNAs with 5'-triphosphate. This piqued our curiosity about whether N. equitans histidyl-tRNA synthetase (NeHisRS) prefers tRNA
with 5'-triphosphate. We show herein that G-1 is still the major recognition element for NeHisRS. However, unlike other prokaryotic HisRSs, which strongly prefer tRNA
with C73, this enzyme shows almost the same preference for C73 and A73. Most intriguingly, NeHisRS still prefers 5'-monophosphate over 5'-triphosphate. It thus appears that the preference of HisRS for tRNA
with 5'-monophosphate emerged very early in evolution.</description><identifier>ISSN: 2165-0497</identifier><identifier>EISSN: 2165-0497</identifier><identifier>DOI: 10.1128/spectrum.04621-22</identifier><identifier>PMID: 36840576</identifier><language>eng</language><publisher>United States</publisher><ispartof>Microbiology spectrum, 2023-04, Vol.11 (2), p.e0462122</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c1562-443de2f9beb26e9e3e3ae0c91d369e9ac5f3d19eb14375caf13f7ed85ce580313</citedby><cites>FETCH-LOGICAL-c1562-443de2f9beb26e9e3e3ae0c91d369e9ac5f3d19eb14375caf13f7ed85ce580313</cites><orcidid>0000-0002-7104-1307</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,860,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/36840576$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Frances Yap, M.-N.</contributor><creatorcontrib>Ivanesthi, Indira Rizqita</creatorcontrib><creatorcontrib>Rida, Gita Riswana Nawung</creatorcontrib><creatorcontrib>Setiawibawa, Aditya Aryandi</creatorcontrib><creatorcontrib>Tseng, Yi-Kuan</creatorcontrib><creatorcontrib>Muammar, Arief</creatorcontrib><creatorcontrib>Wang, Chien-Chia</creatorcontrib><title>Recognition of tRNA His in an RNase P-Free Nanoarchaeum</title><title>Microbiology spectrum</title><addtitle>Microbiol Spectr</addtitle><description>The 5' extra guanosine with 5'-monophosphate at position -1 (G-1) of tRNA
(p-tRNA
) is a nearly universal feature that establishes tRNA
identity. G-1 is either genome encoded and retained after processing by RNase P (RNase P) or posttranscriptionally incorporated by tRNA
guanylyltransferase (Thg1) after RNase P cleavage. However, RNase P is not found in the hyperthermophilic archaeum Nanoarchaeum equitans; instead, all of its tRNAs, including tRNA
, are transcribed as leaderless tRNAs with 5'-triphosphate (ppp-tRNAs). How N. equitans histidyl-tRNA synthetase (NeHisRS) recognizes its cognate tRNA (NetRNA
) is of particular interest. In this paper, we show that G-1 serves as the major identity element of NetRNA
, with its anticodon performing a similar role, though to a lesser extent. Moreover, NeHisRS distinctly preferred p-tRNA
over ppp-tRNA
(~5-fold difference). Unlike other prokaryotic HisRSs, which strongly prefer tRNA
with C73, this enzyme could charge tRNAs
with A73 and C73 with nearly equal efficiency. As a result, mutation at the C73-recognition amino acid residue Q112 had only a minor effect (<2-fold reduction). This study suggests that NeHisRS has evolved to disregard C73, but it still maintains its evolutionarily preserved preference toward tRNA
with 5'-monophosphate.
Mature tRNA
has, at its 5'-terminus, an extra guanosine with 5'-monophosphate, designated G-1. G-1 is the major recognition element for histidyl-tRNA synthetase (HisRS), regardless of whether it is of eukaryotic or prokaryotic origin. However, in the hyperthermophilic archaeum Nanoarchaeum equitans, all its tRNAs, including tRNA
, are transcribed as leaderless tRNAs with 5'-triphosphate. This piqued our curiosity about whether N. equitans histidyl-tRNA synthetase (NeHisRS) prefers tRNA
with 5'-triphosphate. We show herein that G-1 is still the major recognition element for NeHisRS. However, unlike other prokaryotic HisRSs, which strongly prefer tRNA
with C73, this enzyme shows almost the same preference for C73 and A73. Most intriguingly, NeHisRS still prefers 5'-monophosphate over 5'-triphosphate. It thus appears that the preference of HisRS for tRNA
with 5'-monophosphate emerged very early in evolution.</description><issn>2165-0497</issn><issn>2165-0497</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><recordid>eNpNkMtOwzAURC0EolXpB7BB_gEXXzt24mVVUYpUBRTBOnKcawgiD9nJgr8HWopYzWzOSHMIuQa-AhDZbRzQjWFqVzzRApgQZ2QuQCvGE5Oe_-szsozxnXMOwJVQ4pLMpM4SrlI9J2mBrn_tmrHpO9p7Ohb5mu6aSJuO2o4WuY1In9g2INLcdr0N7s3i1F6RC28_Ii5_c0FetnfPmx3bP94_bNZ75kBpwZJE1ii8qbASGg1KlBa5M1BLbdBYp7yswWAFiUyVsx6kT7HOlEOVcQlyQeC460IfY0BfDqFpbfgsgZc_HsqTh_LgoRTim7k5MsNUtVj_EafX8guTAFmx</recordid><startdate>20230413</startdate><enddate>20230413</enddate><creator>Ivanesthi, Indira Rizqita</creator><creator>Rida, Gita Riswana Nawung</creator><creator>Setiawibawa, Aditya Aryandi</creator><creator>Tseng, Yi-Kuan</creator><creator>Muammar, Arief</creator><creator>Wang, Chien-Chia</creator><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><orcidid>https://orcid.org/0000-0002-7104-1307</orcidid></search><sort><creationdate>20230413</creationdate><title>Recognition of tRNA His in an RNase P-Free Nanoarchaeum</title><author>Ivanesthi, Indira Rizqita ; Rida, Gita Riswana Nawung ; Setiawibawa, Aditya Aryandi ; Tseng, Yi-Kuan ; Muammar, Arief ; Wang, Chien-Chia</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c1562-443de2f9beb26e9e3e3ae0c91d369e9ac5f3d19eb14375caf13f7ed85ce580313</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ivanesthi, Indira Rizqita</creatorcontrib><creatorcontrib>Rida, Gita Riswana Nawung</creatorcontrib><creatorcontrib>Setiawibawa, Aditya Aryandi</creatorcontrib><creatorcontrib>Tseng, Yi-Kuan</creatorcontrib><creatorcontrib>Muammar, Arief</creatorcontrib><creatorcontrib>Wang, Chien-Chia</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><jtitle>Microbiology spectrum</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ivanesthi, Indira Rizqita</au><au>Rida, Gita Riswana Nawung</au><au>Setiawibawa, Aditya Aryandi</au><au>Tseng, Yi-Kuan</au><au>Muammar, Arief</au><au>Wang, Chien-Chia</au><au>Frances Yap, M.-N.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Recognition of tRNA His in an RNase P-Free Nanoarchaeum</atitle><jtitle>Microbiology spectrum</jtitle><addtitle>Microbiol Spectr</addtitle><date>2023-04-13</date><risdate>2023</risdate><volume>11</volume><issue>2</issue><spage>e0462122</spage><pages>e0462122-</pages><issn>2165-0497</issn><eissn>2165-0497</eissn><abstract>The 5' extra guanosine with 5'-monophosphate at position -1 (G-1) of tRNA
(p-tRNA
) is a nearly universal feature that establishes tRNA
identity. G-1 is either genome encoded and retained after processing by RNase P (RNase P) or posttranscriptionally incorporated by tRNA
guanylyltransferase (Thg1) after RNase P cleavage. However, RNase P is not found in the hyperthermophilic archaeum Nanoarchaeum equitans; instead, all of its tRNAs, including tRNA
, are transcribed as leaderless tRNAs with 5'-triphosphate (ppp-tRNAs). How N. equitans histidyl-tRNA synthetase (NeHisRS) recognizes its cognate tRNA (NetRNA
) is of particular interest. In this paper, we show that G-1 serves as the major identity element of NetRNA
, with its anticodon performing a similar role, though to a lesser extent. Moreover, NeHisRS distinctly preferred p-tRNA
over ppp-tRNA
(~5-fold difference). Unlike other prokaryotic HisRSs, which strongly prefer tRNA
with C73, this enzyme could charge tRNAs
with A73 and C73 with nearly equal efficiency. As a result, mutation at the C73-recognition amino acid residue Q112 had only a minor effect (<2-fold reduction). This study suggests that NeHisRS has evolved to disregard C73, but it still maintains its evolutionarily preserved preference toward tRNA
with 5'-monophosphate.
Mature tRNA
has, at its 5'-terminus, an extra guanosine with 5'-monophosphate, designated G-1. G-1 is the major recognition element for histidyl-tRNA synthetase (HisRS), regardless of whether it is of eukaryotic or prokaryotic origin. However, in the hyperthermophilic archaeum Nanoarchaeum equitans, all its tRNAs, including tRNA
, are transcribed as leaderless tRNAs with 5'-triphosphate. This piqued our curiosity about whether N. equitans histidyl-tRNA synthetase (NeHisRS) prefers tRNA
with 5'-triphosphate. We show herein that G-1 is still the major recognition element for NeHisRS. However, unlike other prokaryotic HisRSs, which strongly prefer tRNA
with C73, this enzyme shows almost the same preference for C73 and A73. Most intriguingly, NeHisRS still prefers 5'-monophosphate over 5'-triphosphate. It thus appears that the preference of HisRS for tRNA
with 5'-monophosphate emerged very early in evolution.</abstract><cop>United States</cop><pmid>36840576</pmid><doi>10.1128/spectrum.04621-22</doi><orcidid>https://orcid.org/0000-0002-7104-1307</orcidid><oa>free_for_read</oa></addata></record> |
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| title | Recognition of tRNA His in an RNase P-Free Nanoarchaeum |
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