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Structural and interaction analysis of the Rrp5 C-terminal region.

ABSTRACT: Rrp5 is an essential factor during the ribosome biogenesis process. The protein contains a series of 12 S1 RNA-binding domains followed by a TetratricoPeptide Repeat (TPR) domain. In the past, several studies aiming at defining the function of the TPR domain have used nonequivalent Rrp5 constructs, as these protein fragments include not only the TPR module, but also three or four S1 domains. We solved the structure of the Rrp5 TPR module and demonstrated in vitro that the TPR region alone does not bind RNA, while the three S1 domains preceding the TPR module can associate with homopolymeric RNA. Finally, we tested the association of our Rrp5 constructs with several proposed interactors, in support of cryo-EM-based models. Coordinates:Atomic coordinates and structure factors have been deposited to the Protein Data Bank under the accession number 5NLG.

SUBMITTER: Perebaskine N

PROVIDER: S-EPMC6168700 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature

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Structural and interaction analysis of the Rrp5 C-terminal region.

Pérébaskine Natacha N Thore Stéphane S Fribourg Sébastien S

FEBS open bio 20180830 10

Rrp5 is an essential factor during the ribosome biogenesis process. The protein contains a series of 12 S1 RNA-binding domains followed by a TetratricoPeptide Repeat (TPR) domain. In the past, several studies aiming at defining the function of the TPR domain have used nonequivalent Rrp5 constructs, as these protein fragments include not only the TPR module, but also three or four S1 domains. We solved the structure of the Rrp5 TPR module and demonstrated <i>in vitro</i> that the TPR region alone ...[more]

PMID: 30338212

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