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Crystal structure of Mil (Mth680): internal duplication and similarity between the Imp4/Brix domain and the anticodon-binding domain of class IIa aminoacyl-tRNA synthetases.

Ng CL, Waterman D, Koonin EV, Antson AA, Ortiz-Lombardía M
EMBO Rep 6 140-6 (2005)
Cited: 12 times
EuropePMC logo PMID: 15654320

Abstract

Proteins of the Imp4/Brix superfamily are involved in ribosomal RNA processing, an essential function in all cells. We report the first structure of an Imp4/Brix superfamily protein, the Mil (for Methanothermobacter thermautotrophicus Imp4-like) protein (gene product Mth680), from the archaeon M. thermautotrophicus. The amino- and carboxy-terminal halves of Mil show significant structural similarity to one another, suggesting an origin by means of an ancestral duplication. Both halves show the same fold as the anticodon-binding domain of class IIa aminoacyl-tRNA synthetases, with greater conservation seen in the N-terminal half. This structural similarity, together with the charge distribution in Mil, suggests that Imp4/Brix superfamily proteins could bind single-stranded segments of RNA along a concave surface formed by the N-terminal half of their beta-sheet and a central alpha-helix. The crystal structure of Mil is incompatible with the presence, in the Imp4/Brix domain, of a helix-turn-helix motif that was proposed to comprise the RNA-binding moiety of the Imp4/Brix proteins.

Articles - 1w94 mentioned but not cited (3)

  1. Structural and functional analysis of the Rpf2-Rrs1 complex in ribosome biogenesis. Asano N, Kato K, Nakamura A, Komoda K, Tanaka I, Yao M. Nucleic Acids Res. 43 4746-4757 (2015)
  2. The structure of Rpf2-Rrs1 explains its role in ribosome biogenesis. Kharde S, Calviño FR, Gumiero A, Wild K, Sinning I. Nucleic Acids Res. 43 7083-7095 (2015)
  3. Crystal structure of Mil (Mth680): internal duplication and similarity between the Imp4/Brix domain and the anticodon-binding domain of class IIa aminoacyl-tRNA synthetases. Ng CL, Waterman D, Koonin EV, Antson AA, Ortiz-Lombardía M. EMBO Rep. 6 140-146 (2005)


Reviews citing this publication (1)

  1. Assembly and nuclear export of pre-ribosomal particles in budding yeast. Gerhardy S, Menet AM, Peña C, Petkowski JJ, Panse VG. Chromosoma 123 327-344 (2014)

Articles citing this publication (8)

  1. Structural insights into the transcriptional and translational roles of Ebp1. Monie TP, Perrin AJ, Birtley JR, Sweeney TR, Karakasiliotis I, Chaudhry Y, Roberts LO, Matthews S, Goodfellow IG, Curry S. EMBO J. 26 3936-3944 (2007)
  2. Chaperoning 5S RNA assembly. Madru C, Lebaron S, Blaud M, Delbos L, Pipoli J, Pasmant E, Réty S, Leulliot N. Genes Dev. 29 1432-1446 (2015)
  3. Mitochondrial tRNAs as light strand replication origins: similarity between anticodon loops and the loop of the light strand replication origin predicts initiation of DNA replication. Seligmann H. BioSystems 99 85-93 (2010)
  4. Mitochondrial tRNA sequences as unusual replication origins: pathogenic implications for Homo sapiens. Seligmann H, Krishnan NM, Rao BJ. J. Theor. Biol. 243 375-385 (2006)
  5. Cryo-EM structure of an early precursor of large ribosomal subunit reveals a half-assembled intermediate. Zhou D, Zhu X, Zheng S, Tan D, Dong MQ, Ye K. Protein Cell 10 120-130 (2019)
  6. Bacterial calpains and the evolution of the calpain (C2) family of peptidases. Rawlings ND. Biol. Direct 10 66 (2015)
  7. Mpp10 represents a platform for the interaction of multiple factors within the 90S pre-ribosome. Sá-Moura B, Kornprobst M, Kharde S, Ahmed YL, Stier G, Kunze R, Sinning I, Hurt E. PLoS ONE 12 e0183272 (2017)
  8. The U3 small nucleolar ribonucleoprotein component Imp4p is a telomeric DNA-binding protein. Hsieh YC, Tu PJ, Lee YY, Kuo CC, Lin YC, Wu CF, Lin JJ. Biochem. J. 408 387-393 (2007)


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