Academic Journal
Functional role and ribosomal position of the unique N-terminal region of DHX29, a factor required for initiation on structured mammalian mRNAs
العنوان: | Functional role and ribosomal position of the unique N-terminal region of DHX29, a factor required for initiation on structured mammalian mRNAs |
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المؤلفون: | Sweeney, Trevor R, Dhote, Vidya, Guca, Ewelina, Hellen, Christopher U T, Hashem, Yaser, Pestova, Tatyana V |
المساهمون: | NIH, European Research Council |
المصدر: | Nucleic Acids Research ; volume 49, issue 22, page 12955-12969 ; ISSN 0305-1048 1362-4962 |
بيانات النشر: | Oxford University Press (OUP) |
سنة النشر: | 2021 |
الوصف: | Translation initiation on structured mammalian mRNAs requires DHX29, a DExH protein that comprises a unique 534-aa-long N-terminal region (NTR) and a common catalytic DExH core. DHX29 binds to 40S subunits and possesses 40S-stimulated NTPase activity essential for its function. In the cryo-EM structure of DHX29-bound 43S preinitiation complexes, the main DHX29 density resides around the tip of helix 16 of 18S rRNA, from which it extends through a linker to the subunit interface forming an intersubunit domain next to the eIF1A binding site. Although a DExH core model can be fitted to the main density, the correlation between the remaining density and the NTR is unknown. Here, we present a model of 40S-bound DHX29, supported by directed hydroxyl radical cleavage data, showing that the intersubunit domain comprises a dsRNA-binding domain (dsRBD, aa 377–448) whereas linker corresponds to the long α-helix (aa 460–512) that follows the dsRBD. We also demonstrate that the N-terminal α-helix and the following UBA-like domain form a four-helix bundle (aa 90–166) that constitutes a previously unassigned section of the main density and resides between DHX29’s C-terminal α-helix and the linker. In vitro reconstitution experiments revealed the critical and specific roles of these NTR elements for DHX29’s function. |
نوع الوثيقة: | article in journal/newspaper |
اللغة: | English |
DOI: | 10.1093/nar/gkab1192 |
الاتاحة: | https://doi.org/10.1093/nar/gkab1192 https://academic.oup.com/nar/article-pdf/49/22/12955/41811367/gkab1192.pdf |
Rights: | https://creativecommons.org/licenses/by/4.0/ |
رقم الانضمام: | edsbas.119276A7 |
قاعدة البيانات: | BASE |
DOI: | 10.1093/nar/gkab1192 |
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