Academic Journal

Functional role and ribosomal position of the unique N-terminal region of DHX29, a factor required for initiation on structured mammalian mRNAs

التفاصيل البيبلوغرافية
العنوان: Functional role and ribosomal position of the unique N-terminal region of DHX29, a factor required for initiation on structured mammalian mRNAs
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