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Article ; Online: Intra- and inter-molecular regulation by intrinsically-disordered regions governs PUF protein RNA binding.

Qiu, Chen / Zhang, Zihan / Wine, Robert N / Campbell, Zachary T / Zhang, Jun / Hall, Traci M Tanaka

2023 Volume 14, Issue 1, Page(s) 7323

Abstract: PUF proteins are characterized by globular RNA-binding domains. They also interact with partner proteins that modulate their RNA-binding activities. Caenorhabditis elegans PUF protein fem-3 binding factor-2 (FBF-2) partners with intrinsically disordered ... ...

Abstract	PUF proteins are characterized by globular RNA-binding domains. They also interact with partner proteins that modulate their RNA-binding activities. Caenorhabditis elegans PUF protein fem-3 binding factor-2 (FBF-2) partners with intrinsically disordered Lateral Signaling Target-1 (LST-1) to regulate target mRNAs in germline stem cells. Here, we report that an intrinsically disordered region (IDR) at the C-terminus of FBF-2 autoinhibits its RNA-binding affinity by increasing the off rate for RNA binding. Moreover, the FBF-2 C-terminal region interacts with its globular RNA-binding domain at the same site where LST-1 binds. This intramolecular interaction restrains an electronegative cluster of amino acid residues near the 5' end of the bound RNA to inhibit RNA binding. LST-1 binding in place of the FBF-2 C-terminus therefore releases autoinhibition and increases RNA-binding affinity. This regulatory mechanism, driven by IDRs, provides a biochemical and biophysical explanation for the interdependence of FBF-2 and LST-1 in germline stem cell self-renewal.
MeSH term(s)	Animals ; RNA/genetics ; RNA/metabolism ; Caenorhabditis elegans Proteins/metabolism ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/metabolism ; Protein Binding ; RNA, Messenger/genetics ; RNA, Messenger/metabolism
Chemical Substances	RNA (63231-63-0) ; Caenorhabditis elegans Proteins ; RNA, Messenger ; LST-1 protein, C elegans
Language	English
Publishing date	2023-11-13
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-023-43098-1
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: De-coding and re-coding RNA recognition by PUF and PPR repeat proteins.

Hall, Traci M Tanaka

Current opinion in structural biology

2016 Volume 36, Page(s) 116–121

Abstract: PUF and PPR proteins are two families of α-helical repeat proteins that recognize single-stranded RNA sequences. Both protein families hold promise as scaffolds for designed RNA-binding domains. A modular protein RNA recognition code was apparent from ... ...

Abstract	PUF and PPR proteins are two families of α-helical repeat proteins that recognize single-stranded RNA sequences. Both protein families hold promise as scaffolds for designed RNA-binding domains. A modular protein RNA recognition code was apparent from the first crystal structures of a PUF protein in complex with RNA, and recent studies continue to advance our understanding of natural PUF protein recognition (de-coding) and our ability to engineer specificity (re-coding). Degenerate recognition motifs make de-coding specificity of individual PPR proteins challenging. Nevertheless, re-coding PPR protein specificity using a consensus recognition code has been successful.
MeSH term(s)	Binding Sites ; Models, Molecular ; Nucleic Acid Conformation ; Nucleotide Motifs ; Protein Binding ; Protein Conformation ; RNA/chemistry ; RNA/metabolism ; RNA-Binding Proteins/chemistry ; RNA-Binding Proteins/metabolism ; Structure-Activity Relationship
Chemical Substances	RNA-Binding Proteins ; RNA (63231-63-0)
Language	English
Publishing date	2016-02-11
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Review
ZDB-ID	1068353-7
ISSN	1879-033X ; 0959-440X
ISSN (online)	1879-033X
ISSN	0959-440X
DOI	10.1016/j.sbi.2016.01.010
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Article ; Online: Bipartite interaction sites differentially modulate RNA-binding affinity of a protein complex essential for germline stem cell self-renewal.

Qiu, Chen / Wine, Robert N / Campbell, Zachary T / Hall, Traci M Tanaka

Nucleic acids research

2021 Volume 50, Issue 1, Page(s) 536–548

Abstract: In C. elegans, PUF proteins promote germline stem cell self-renewal. Their functions hinge on partnerships with two proteins that are redundantly required for stem cell maintenance. Here we focus on understanding how the essential partner protein, LST-1, ...

Abstract	In C. elegans, PUF proteins promote germline stem cell self-renewal. Their functions hinge on partnerships with two proteins that are redundantly required for stem cell maintenance. Here we focus on understanding how the essential partner protein, LST-1, modulates mRNA regulation by the PUF protein, FBF-2. LST-1 contains two nonidentical sites of interaction with FBF-2, LST-1 A and B. Our crystal structures of complexes of FBF-2, LST-1 A, and RNA visualize how FBF-2 associates with LST-1 A versus LST-1 B. One commonality is that FBF-2 contacts the conserved lysine and leucine side chains in the KxxL motifs in LST-1 A and B. A key difference is that FBF-2 forms unique contacts with regions N- and C-terminal to the KxxL motif. Consequently, LST-1 A does not modulate the RNA-binding affinity of FBF-2, whereas LST-1 B decreases RNA-binding affinity of FBF-2. The N-terminal region of LST-1 B, which binds near the 5' end of RNA elements, is essential to modulate FBF-2 RNA-binding affinity, while the C-terminal residues of LST-1 B contribute strong binding affinity to FBF-2. We conclude that LST-1 has the potential to impact which mRNAs are regulated depending on the precise nature of engagement through its functionally distinct FBF binding sites.
MeSH term(s)	Animals ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/metabolism ; Protein Binding ; RNA, Messenger/metabolism ; RNA-Binding Proteins/metabolism
Chemical Substances	Caenorhabditis elegans Proteins ; LST-1 protein, C elegans ; RNA, Messenger ; RNA-Binding Proteins ; fem-3-binding protein, C elegans
Language	English
Publishing date	2021-12-15
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkab1220
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Article ; Online: The translational repressor Glorund uses interchangeable RNA recognition domains to recognize Drosophila nanos.

Warden, Meghan S / DeRose, Eugene F / Tamayo, Joel V / Mueller, Geoffrey A / Gavis, Elizabeth R / Hall, Traci M Tanaka

Nucleic acids research

2023 Volume 51, Issue 16, Page(s) 8836–8849

Abstract: The Drosophila melanogaster protein Glorund (Glo) represses nanos (nos) translation and uses its quasi-RNA recognition motifs (qRRMs) to recognize both G-tract and structured UA-rich motifs within the nos translational control element (TCE). We showed ... ...

Abstract	The Drosophila melanogaster protein Glorund (Glo) represses nanos (nos) translation and uses its quasi-RNA recognition motifs (qRRMs) to recognize both G-tract and structured UA-rich motifs within the nos translational control element (TCE). We showed previously that each of the three qRRMs is multifunctional, capable of binding to G-tract and UA-rich motifs, yet if and how the qRRMs combine to recognize the nos TCE remained unclear. Here we determined solution structures of a nos TCEI_III RNA containing the G-tract and UA-rich motifs. The RNA structure demonstrated that a single qRRM is physically incapable of recognizing both RNA elements simultaneously. In vivo experiments further indicated that any two qRRMs are sufficient to repress nos translation. We probed interactions of Glo qRRMs with TCEI_III RNA using NMR paramagnetic relaxation experiments. Our in vitro and in vivo data support a model whereby tandem Glo qRRMs are indeed multifunctional and interchangeable for recognition of TCE G-tract or UA-rich motifs. This study illustrates how multiple RNA recognition modules within an RNA-binding protein may combine to diversify the RNAs that are recognized and regulated.
MeSH term(s)	Animals ; Drosophila/genetics ; Drosophila melanogaster/genetics ; Drosophila melanogaster/metabolism ; Drosophila Proteins/metabolism ; Protein Biosynthesis ; RNA/chemistry
Chemical Substances	Drosophila Proteins ; RNA (63231-63-0) ; Glo protein, Drosophila ; nos protein, Drosophila (142661-95-8)
Language	English
Publishing date	2023-09-19
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkad586
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Article ; Online: Preparation of cooperative RNA recognition complexes for crystallographic structural studies.

Qiu, Chen / Goldstrohm, Aaron C / Tanaka Hall, Traci M

Methods in enzymology

2019 Volume 623, Page(s) 1–22

Abstract: It is essential that mRNA-binding proteins recognize specific motifs in target mRNAs to control their processing, localization, and expression. Although mRNAs are typically targets of many different regulatory factors, our understanding of how they work ... ...

Abstract	It is essential that mRNA-binding proteins recognize specific motifs in target mRNAs to control their processing, localization, and expression. Although mRNAs are typically targets of many different regulatory factors, our understanding of how they work together is limited. In some cases, RNA-binding proteins work cooperatively to regulate an mRNA target. A classic example is Drosophila melanogaster Pumilio (Pum) and Nanos (Nos). Pum is a sequence-specific RNA-binding protein. Nos also binds RNA, but interaction with some targets requires Pum to bind first. We recently determined crystal structures of complexes of Pum and Nos with two different target RNA sequences. A crystal structure in complex with the hunchback mRNA element showed how Pum and Nos together can recognize an extended RNA sequence with Nos binding to an A/U-rich sequence 5' of the Pum sequence element. Nos also enables recognition of elements that contain an A/U-rich 5' sequence, but imperfectly match the Pum sequence element. We determined a crystal structure of Pum and Nos in complex with the Cyclin B mRNA element, which demonstrated how Nos clamps the Pum-RNA complex and enables recognition of the imperfect element. Here, we describe methods for expression and purification of stable Pum-Nos-RNA complexes for crystallization, details of the crystallization and structure determination, and guidance on how to analyze protein-RNA structures and evaluate structure-driven hypotheses. We aim to provide tips and guidance that can be applied to other protein-RNA complexes. With hundreds of mRNA-binding proteins identified, combinatorial control is likely to be common, and much work remains to understand them structurally.
MeSH term(s)	Animals ; Binding Sites ; Crystallography/methods ; Crystallography, X-Ray/methods ; Drosophila Proteins/chemistry ; Drosophila Proteins/metabolism ; Drosophila melanogaster/chemistry ; Drosophila melanogaster/metabolism ; Models, Molecular ; Nucleic Acid Conformation ; Protein Binding ; Protein Conformation ; RNA/chemistry ; RNA/metabolism ; RNA, Messenger/chemistry ; RNA, Messenger/metabolism ; RNA-Binding Proteins/chemistry ; RNA-Binding Proteins/metabolism
Chemical Substances	Drosophila Proteins ; RNA, Messenger ; RNA-Binding Proteins ; pum protein, Drosophila ; nos protein, Drosophila (142661-95-8) ; RNA (63231-63-0)
Language	English
Publishing date	2019-05-02
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural
ISSN	1557-7988
ISSN (online)	1557-7988
DOI	10.1016/bs.mie.2019.04.001
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Article ; Online: Expanding the RNA-recognition code of PUF proteins.

Hall, Traci M Tanaka

Nature structural & molecular biology

2014 Volume 21, Issue 8, Page(s) 653–655

MeSH term(s)	Humans ; RNA, Messenger/metabolism ; RNA-Binding Proteins/genetics
Chemical Substances	RNA, Messenger ; RNA-Binding Proteins
Language	English
Publishing date	2014-06-03
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	2126708-X
ISSN	1545-9985 ; 1545-9993
ISSN (online)	1545-9985
ISSN	1545-9993
DOI	10.1038/nsmb.2863
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Zs.A 4101: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Structural basis of microRNA biogenesis by Dicer-1 and its partner protein Loqs-PB.

Jouravleva, Karina / Golovenko, Dmitrij / Demo, Gabriel / Dutcher, Robert C / Hall, Traci M Tanaka / Zamore, Phillip D / Korostelev, Andrei A

Molecular cell

2022 Volume 82, Issue 21, Page(s) 4049–4063.e6

Abstract: In animals and plants, Dicer enzymes collaborate with double-stranded RNA-binding domain (dsRBD) proteins to convert precursor-microRNAs (pre-miRNAs) into miRNA duplexes. We report six cryo-EM structures of Drosophila Dicer-1 that show how Dicer-1 and ... ...

Abstract	In animals and plants, Dicer enzymes collaborate with double-stranded RNA-binding domain (dsRBD) proteins to convert precursor-microRNAs (pre-miRNAs) into miRNA duplexes. We report six cryo-EM structures of Drosophila Dicer-1 that show how Dicer-1 and its partner Loqs‑PB cooperate (1) before binding pre-miRNA, (2) after binding and in a catalytically competent state, (3) after nicking one arm of the pre-miRNA, and (4) following complete dicing and initial product release. Our reconstructions suggest that pre-miRNA binds a rare, open conformation of the Dicer‑1⋅Loqs‑PB heterodimer. The Dicer-1 dsRBD and three Loqs‑PB dsRBDs form a tight belt around the pre-miRNA, distorting the RNA helix to place the scissile phosphodiester bonds in the RNase III active sites. Pre-miRNA cleavage shifts the dsRBDs and partially closes Dicer-1, which may promote product release. Our data suggest a model for how the Dicer‑1⋅Loqs‑PB complex affects a complete cycle of pre-miRNA recognition, stepwise endonuclease cleavage, and product release.
MeSH term(s)	Animals ; Ribonuclease III/genetics ; Ribonuclease III/metabolism ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; RNA-Binding Proteins/metabolism ; Drosophila/genetics ; MicroRNAs/genetics ; MicroRNAs/metabolism
Chemical Substances	Ribonuclease III (EC 3.1.26.3) ; Drosophila Proteins ; RNA-Binding Proteins ; MicroRNAs
Language	English
Publishing date	2022-09-30
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2022.09.002
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Zs.A 5055: Show issues

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Article ; Online: High-resolution structures of the SAMHD1 dGTPase homolog from Leeuwenhoekiella blandensis reveal a novel mechanism of allosteric activation by dATP.

Klemm, Bradley P / Sikkema, Andrew P / Hsu, Allen L / Horng, James C / Hall, Traci M Tanaka / Borgnia, Mario J / Schaaper, Roel M

The Journal of biological chemistry

2022 Volume 298, Issue 7, Page(s) 102073

Abstract: Deoxynucleoside triphosphate (dNTP) triphosphohydrolases (dNTPases) are important enzymes that may perform multiple functions in the cell, including regulating the dNTP pools and contributing to innate immunity against viruses. Among the homologs that ... ...

Abstract	Deoxynucleoside triphosphate (dNTP) triphosphohydrolases (dNTPases) are important enzymes that may perform multiple functions in the cell, including regulating the dNTP pools and contributing to innate immunity against viruses. Among the homologs that are best studied are human sterile alpha motif and HD domain-containing protein 1 (SAMHD1), a tetrameric dNTPase, and the hexameric Escherichia coli dGTPase; however, it is unclear whether these are representative of all dNTPases given their wide distribution throughout life. Here, we investigated a hexameric homolog from the marine bacterium Leeuwenhoekiella blandensis, revealing that it is a dGTPase that is subject to allosteric activation by dATP, specifically. Allosteric regulation mediated solely by dATP represents a novel regulatory feature among dNTPases that may facilitate maintenance of cellular dNTP pools in L. blandensis. We present high-resolution X-ray crystallographic structures (1.80-2.26 Å) in catalytically important conformations as well as cryo-EM structures (2.1-2.7 Å) of the enzyme bound to dGTP and dATP ligands. The structures, the highest resolution cryo-EM structures of any SAMHD1-like dNTPase to date, reveal an intact metal-binding site with the dGTP substrate coordinated to three metal ions. These structural and biochemical data yield insights into the catalytic mechanism and support a conserved catalytic mechanism for the tetrameric and hexameric dNTPase homologs. We conclude that the allosteric activation by dATP appears to rely on structural connectivity between the allosteric and active sites, as opposed to the changes in oligomeric state upon ligand binding used by SAMHD1.
MeSH term(s)	Allosteric Regulation/physiology ; Escherichia coli/metabolism ; Flavobacteriaceae ; Humans ; Models, Molecular ; Monomeric GTP-Binding Proteins/metabolism ; SAM Domain and HD Domain-Containing Protein 1/metabolism
Chemical Substances	SAM Domain and HD Domain-Containing Protein 1 (EC 3.1.5.-) ; SAMHD1 protein, human (EC 3.1.5.-) ; Monomeric GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2022-05-26
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2022.102073
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Uc I Zs.108: Show issues

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Article ; Online: H/ACA snoRNA levels are regulated during stem cell differentiation.

McCann, Kathleen L / Kavari, Sanam L / Burkholder, Adam B / Phillips, Bart T / Hall, Traci M Tanaka

Nucleic acids research

2020 Volume 48, Issue 15, Page(s) 8686–8703

Abstract: H/ACA small nucleolar RNAs (snoRNAs) guide pseudouridylation as part of a small nucleolar ribonucleoprotein complex (snoRNP). Disruption of H/ACA snoRNA levels in stem cells impairs pluripotency, yet it remains unclear how H/ACA snoRNAs contribute to ... ...

Abstract	H/ACA small nucleolar RNAs (snoRNAs) guide pseudouridylation as part of a small nucleolar ribonucleoprotein complex (snoRNP). Disruption of H/ACA snoRNA levels in stem cells impairs pluripotency, yet it remains unclear how H/ACA snoRNAs contribute to differentiation. To determine if H/ACA snoRNA levels are dynamic during differentiation, we comprehensively profiled H/ACA snoRNA abundance in multiple murine cell types and during differentiation in three cellular models, including mouse embryonic stem cells and mouse myoblasts. We determined that the profiles of H/ACA snoRNA abundance are cell-type specific, and we identified a subset of snoRNAs that are specifically regulated during differentiation. Additionally, we demonstrated that a decrease in Snora27 abundance upon differentiation corresponds to a decrease in pseudouridylation of its target site within the E-site transfer RNA (tRNA) binding region of the 28S ribosomal RNA (rRNA) in the large ribosomal subunit. Together, these data point toward a potential model in which H/ACA snoRNAs are specifically regulated during differentiation to alter pseudouridylation and fine tune ribosome function.
MeSH term(s)	Animals ; Base Sequence/genetics ; Cell Differentiation/genetics ; Mice ; Mouse Embryonic Stem Cells ; Myoblasts/metabolism ; Nucleic Acid Conformation ; Pseudouridine/genetics ; RNA, Ribosomal, 28S/genetics ; RNA, Small Nucleolar/genetics ; Ribonucleoproteins, Small Nucleolar/genetics ; Ribosomes/genetics
Chemical Substances	RNA, Ribosomal, 28S ; RNA, Small Nucleolar ; Ribonucleoproteins, Small Nucleolar ; Pseudouridine (1445-07-4)
Language	English
Publishing date	2020-07-24
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkaa612
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Zs.A 1067: Show issues

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Article ; Online: Pentatricopeptide repeats of protein-only RNase P use a distinct mode to recognize conserved bases and structural elements of pre-tRNA.

Teramoto, Takamasa / Kaitany, Kipchumba J / Kakuta, Yoshimitsu / Kimura, Makoto / Fierke, Carol A / Hall, Traci M Tanaka

Nucleic acids research

2020 Volume 48, Issue 21, Page(s) 11815–11826

Abstract: Pentatricopeptide repeat (PPR) motifs are α-helical structures known for their modular recognition of single-stranded RNA sequences with each motif in a tandem array binding to a single nucleotide. Protein-only RNase P 1 (PRORP1) in Arabidopsis thaliana ... ...

Abstract	Pentatricopeptide repeat (PPR) motifs are α-helical structures known for their modular recognition of single-stranded RNA sequences with each motif in a tandem array binding to a single nucleotide. Protein-only RNase P 1 (PRORP1) in Arabidopsis thaliana is an endoribonuclease that uses its PPR domain to recognize precursor tRNAs (pre-tRNAs) as it catalyzes removal of the 5'-leader sequence from pre-tRNAs with its NYN metallonuclease domain. To gain insight into the mechanism by which PRORP1 recognizes tRNA, we determined a crystal structure of the PPR domain in complex with yeast tRNAPhe at 2.85 Å resolution. The PPR domain of PRORP1 bound to the structurally conserved elbow of tRNA and recognized conserved structural features of tRNAs using mechanisms that are different from the established single-stranded RNA recognition mode of PPR motifs. The PRORP1 PPR domain-tRNAPhe structure revealed a conformational change of the PPR domain upon tRNA binding and moreover demonstrated the need for pronounced overall flexibility in the PRORP1 enzyme conformation for substrate recognition and catalysis. The PRORP1 PPR motifs have evolved strategies for protein-tRNA interaction analogous to tRNA recognition by the RNA component of ribonucleoprotein RNase P and other catalytic RNAs, indicating convergence on a common solution for tRNA substrate recognition.
MeSH term(s)	Amino Acid Sequence ; Arabidopsis/genetics ; Arabidopsis/metabolism ; Arabidopsis Proteins/chemistry ; Arabidopsis Proteins/genetics ; Arabidopsis Proteins/metabolism ; Binding Sites ; Cloning, Molecular ; Conserved Sequence ; Crystallography, X-Ray ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Gene Expression ; Genetic Vectors/chemistry ; Genetic Vectors/metabolism ; Kinetics ; Models, Molecular ; Nucleic Acid Conformation ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Interaction Domains and Motifs ; RNA Precursors/chemistry ; RNA Precursors/genetics ; RNA Precursors/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Ribonuclease P/chemistry ; Ribonuclease P/genetics ; Ribonuclease P/metabolism ; Sequence Alignment ; Substrate Specificity
Chemical Substances	Arabidopsis Proteins ; RNA Precursors ; Recombinant Proteins ; PRORP1 protein, Arabidopsis (EC 3.1.26.5) ; Ribonuclease P (EC 3.1.26.5)
Language	English
Publishing date	2020-07-27
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkaa627
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