Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 366, Issue 1, Pages 155-164Publisher
ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2006.11.024
Keywords
tRNA splicing endonuclease; NMR solution structure; homodimeric protein assembly; beta barrel dimer interface
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Funding
- NCRR NIH HHS [P41 RR002301, P41 RR 02301] Funding Source: Medline
- NIGMS NIH HHS [P41 GM 66326, P50 GM064598, P50 GM 64598, U54 GM 074901, P41 GM066326, U54 GM074901] Funding Source: Medline
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Splicing of eukaryal intron-containing tRNAs requires the action of the heterotetrameric splicing endonuclease, which is composed of two catalytic subunits, Sen34 and Sen2, and two structural subunits, Sen15 and Sen54. Here we report the solution structure of the human tRNA splicing endonuclease subunit HsSen15. To facilitate the structure determination, we removed the disordered 35 N-terminal and 14 C-terminal residues of the full-length protein to produce HsSen15(36-157). The structure of HsSen15 (36-157), the first for a subunit of a eukaryal splicing endonuclease, revealed that the protein possesses a novel homodimeric fold. Each monomer consists of three alpha-helices and a mixed antiparallel/parallel beta-sheet, arranged in a topology similar to that of the C-terminal domain of Methano-caldococcus jannaschii endonuclease. The dimeric interface is dominated by a beta-barrel structure, formed by face-to-face packing of two, three-stranded beta-sheets. Each of the beta-sheets results from reciprocal parallel pairing of one beta-strand from one subunit with two other beta-strands from the symmetric subunit. The structural model provides insights into the functional assembly of the human tRNA splicing endonuclease. (c) 2006 Elsevier Ltd. All rights reserved.
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