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Structures of the T. brucei kRNA editing factor MRB1590 reveal unique RNA-binding pore motif contained within an ABC-ATPase fold.

Publication ,  Journal Article
Shaw, PLR; McAdams, NM; Hast, MA; Ammerman, ML; Read, LK; Schumacher, MA
Published in: Nucleic Acids Res
August 18, 2015

Kinetoplastid RNA (kRNA) editing is a process that creates translatable mitochondrial mRNA transcripts from cryptogene encoded RNAs and is unique for kinetoplastids, such as Trypanosoma brucei. In addition to the catalytic 20S editosome, multiple accessory proteins are required for this conversion. Recently, the multiprotein mitochondrial RNA binding complex 1 (MRB1) has emerged as a key player in this process. MRB1 consists of six core proteins but makes dynamic interactions with additional accessory proteins. Here we describe the characterization of one such factor, the 72 kDa MRB1590 protein. In vivo experiments indicate a role for MRB1590 in editing mitochondrial mRNA transcripts, in particular the transcript encoding the ATP synthase subunit 6 (A6). Structural studies show that MRB1590 is dimeric and contains a central ABC-ATPase fold embedded between novel N- and C-terminal regions. The N-terminal domains combine to create a basic pore and biochemical studies indicate residues in this region participate in RNA binding. Structures capturing distinct MRB1590 conformations reveal that the RNA binding pore adopts closed and open states, with the latter able to accommodate RNA. Based on these findings, implications for MRB1590 function are discussed.

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Published In

Nucleic Acids Res

DOI

EISSN

1362-4962

Publication Date

August 18, 2015

Volume

43

Issue

14

Start / End Page

7096 / 7109

Location

England

Related Subject Headings

  • Trypanosoma brucei brucei
  • RNA-Binding Proteins
  • RNA, Protozoan
  • RNA, Mitochondrial
  • RNA Editing
  • RNA
  • Protozoan Proteins
  • Protein Structure, Tertiary
  • Protein Multimerization
  • Poly U
 

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Shaw, P. L. R., McAdams, N. M., Hast, M. A., Ammerman, M. L., Read, L. K., & Schumacher, M. A. (2015). Structures of the T. brucei kRNA editing factor MRB1590 reveal unique RNA-binding pore motif contained within an ABC-ATPase fold. Nucleic Acids Res, 43(14), 7096–7109. https://doi.org/10.1093/nar/gkv647
Shaw, Porsha L. R., Natalie M. McAdams, Michael A. Hast, Michelle L. Ammerman, Laurie K. Read, and Maria A. Schumacher. “Structures of the T. brucei kRNA editing factor MRB1590 reveal unique RNA-binding pore motif contained within an ABC-ATPase fold.Nucleic Acids Res 43, no. 14 (August 18, 2015): 7096–7109. https://doi.org/10.1093/nar/gkv647.
Shaw PLR, McAdams NM, Hast MA, Ammerman ML, Read LK, Schumacher MA. Structures of the T. brucei kRNA editing factor MRB1590 reveal unique RNA-binding pore motif contained within an ABC-ATPase fold. Nucleic Acids Res. 2015 Aug 18;43(14):7096–109.
Shaw, Porsha L. R., et al. “Structures of the T. brucei kRNA editing factor MRB1590 reveal unique RNA-binding pore motif contained within an ABC-ATPase fold.Nucleic Acids Res, vol. 43, no. 14, Aug. 2015, pp. 7096–109. Pubmed, doi:10.1093/nar/gkv647.
Shaw PLR, McAdams NM, Hast MA, Ammerman ML, Read LK, Schumacher MA. Structures of the T. brucei kRNA editing factor MRB1590 reveal unique RNA-binding pore motif contained within an ABC-ATPase fold. Nucleic Acids Res. 2015 Aug 18;43(14):7096–7109.
Journal cover image

Published In

Nucleic Acids Res

DOI

EISSN

1362-4962

Publication Date

August 18, 2015

Volume

43

Issue

14

Start / End Page

7096 / 7109

Location

England

Related Subject Headings

  • Trypanosoma brucei brucei
  • RNA-Binding Proteins
  • RNA, Protozoan
  • RNA, Mitochondrial
  • RNA Editing
  • RNA
  • Protozoan Proteins
  • Protein Structure, Tertiary
  • Protein Multimerization
  • Poly U