Recognition of 2′-O-Methylated 3′-End of piRNA by the PAZ Domain of a Piwi Protein

Publication type:
Journal article
Metadata:
Autoren
  • Bernd Simon
  • John P Kirkpatrick
  • Stephanie Eckhardt
  • Michael Reuter
  • Elsa A Rocha
  • Miguel A Andrade-Navarro
  • Peter Sehr
  • Ramesh S Pillai
  • Teresa Carlomagno
Autoren-URL
https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000287344900007&DestLinkType=FullRecord&DestApp=WOS_CPL
DOI
10.1016/j.str.2010.11.015
eISSN
1878-4186
Externe Identifier
  • Clarivate Analytics Document Solution ID: 721HT
  • PubMed Identifier: 21237665
ISSN
0969-2126
Ausgabe der Veröffentlichung
2
Zeitschrift
STRUCTURE
Paginierung
172 - 180
Datum der Veröffentlichung
2011
Status
Published
Titel
Recognition of 2′-<i>O</i>-Methylated 3′-End of piRNA by the PAZ Domain of a Piwi Protein
Sub types
  • Article
Ausgabe der Zeitschrift
19

Data source: Web of Science (Lite)

Other metadata sources:
Autoren
  • Bernd Simon
  • John P Kirkpatrick
  • Stephanie Eckhardt
  • Michael Reuter
  • Elsa A Rocha
  • Miguel A Andrade-Navarro
  • Peter Sehr
  • Ramesh S Pillai
  • Teresa Carlomagno
DOI
10.1016/j.str.2010.11.015
ISSN
0969-2126
Ausgabe der Veröffentlichung
2
Zeitschrift
Structure
Sprache
en
Paginierung
172 - 180
Datum der Veröffentlichung
2011
Status
Published
Herausgeber
Elsevier BV
Herausgeber URL
http://dx.doi.org/10.1016/j.str.2010.11.015
Datum der Datenerfassung
2024
Titel
Recognition of 2′-O-Methylated 3′-End of piRNA by the PAZ Domain of a Piwi Protein
Ausgabe der Zeitschrift
19

Data source: Crossref

Abstract
Piwi proteins are germline-specific Argonautes that associate with small RNAs called Piwi-interacting RNAs (piRNAs), and together with these RNAs are implicated in transposon silencing. The PAZ domain of Argonaute proteins recognizes the 3'-end of the RNA, which in the case of piRNAs is invariably modified with a 2'-O-methyl group. Here, we present the solution structure of the PAZ domain from the mouse Piwi protein, MIWI, in complex with an 8-mer piRNA mimic. The methyl group is positioned in a hydrophobic cavity made of conserved amino acids from strand β7 and helix α3, where it is contacted by the side chain of methionine-382. Our structure is similar to that of Ago-PAZ, but subtle differences illustrate how the PAZ domain has evolved to accommodate distinct 3' ends from a variety of RNA substrates.
Addresses
  • Structural and Computational Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany.
Autoren
  • Bernd Simon
  • John P Kirkpatrick
  • Stephanie Eckhardt
  • Michael Reuter
  • Elsa A Rocha
  • Miguel A Andrade-Navarro
  • Peter Sehr
  • Ramesh S Pillai
  • Teresa Carlomagno
DOI
10.1016/j.str.2010.11.015
eISSN
1878-4186
Externe Identifier
  • PubMed Identifier: 21237665
Funding acknowledgements
  • European Molecular Biology Laboratory:
  • Agence Nationale de la Recherche:
Open access
false
ISSN
0969-2126
Ausgabe der Veröffentlichung
2
Zeitschrift
Structure (London, England : 1993)
Schlüsselwörter
  • Animals
  • Mice
  • Escherichia coli
  • Methionine
  • Proteins
  • Recombinant Proteins
  • RNA, Small Interfering
  • DNA Transposable Elements
  • Oligonucleotides
  • Surface Plasmon Resonance
  • Evolution, Molecular
  • Gene Silencing
  • Binding Sites
  • Molecular Mimicry
  • Amino Acid Sequence
  • Protein Structure, Tertiary
  • Protein Binding
  • Methylation
  • Molecular Sequence Data
  • Argonaute Proteins
Sprache
eng
Medium
Print-Electronic
Online publication date
2011
Paginierung
172 - 180
Datum der Veröffentlichung
2011
Status
Published
Datum der Datenerfassung
2011
Titel
Recognition of 2'-O-methylated 3'-end of piRNA by the PAZ domain of a Piwi protein.
Sub types
  • Research Support, Non-U.S. Gov't
  • Journal Article
Ausgabe der Zeitschrift
19

Data source: Europe PubMed Central

Abstract
Piwi proteins are germline-specific Argonautes that associate with small RNAs called Piwi-interacting RNAs (piRNAs), and together with these RNAs are implicated in transposon silencing. The PAZ domain of Argonaute proteins recognizes the 3'-end of the RNA, which in the case of piRNAs is invariably modified with a 2'-O-methyl group. Here, we present the solution structure of the PAZ domain from the mouse Piwi protein, MIWI, in complex with an 8-mer piRNA mimic. The methyl group is positioned in a hydrophobic cavity made of conserved amino acids from strand β7 and helix α3, where it is contacted by the side chain of methionine-382. Our structure is similar to that of Ago-PAZ, but subtle differences illustrate how the PAZ domain has evolved to accommodate distinct 3' ends from a variety of RNA substrates.
Date of acceptance
2010
Autoren
  • Bernd Simon
  • John P Kirkpatrick
  • Stephanie Eckhardt
  • Michael Reuter
  • Elsa A Rocha
  • Miguel A Andrade-Navarro
  • Peter Sehr
  • Ramesh S Pillai
  • Teresa Carlomagno
Autoren-URL
https://www.ncbi.nlm.nih.gov/pubmed/21237665
DOI
10.1016/j.str.2010.11.015
eISSN
1878-4186
Ausgabe der Veröffentlichung
2
Zeitschrift
Structure
Schlüsselwörter
  • Amino Acid Sequence
  • Animals
  • Argonaute Proteins
  • Binding Sites
  • DNA Transposable Elements
  • Escherichia coli
  • Evolution, Molecular
  • Gene Silencing
  • Methionine
  • Methylation
  • Mice
  • Molecular Mimicry
  • Molecular Sequence Data
  • Oligonucleotides
  • Protein Binding
  • Protein Structure, Tertiary
  • Proteins
  • RNA, Small Interfering
  • Recombinant Proteins
  • Surface Plasmon Resonance
Sprache
eng
Country
United States
Paginierung
172 - 180
PII
S0969-2126(10)00441-7
Datum der Veröffentlichung
2011
Status
Published
Datum, an dem der Datensatz öffentlich gemacht wurde
2011
Titel
Recognition of 2'-O-methylated 3'-end of piRNA by the PAZ domain of a Piwi protein.
Sub types
  • Journal Article
  • Research Support, Non-U.S. Gov't
Ausgabe der Zeitschrift
19

Data source: PubMed

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