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The RNA-associated proteins MKT1 and MKT1L form alternative PBP1-containing complexes in Trypanosoma brucei

Control of gene expression in kinetoplastids such as trypanosomes depends heavily on RNA-binding proteins that influence mRNA decay and translation. We previously showed that the trypanosome protein MKT1 forms a multicomponent protein complex: MKT1 interacts with PBP1, which in turn recruits LSM12 a...

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Main Authors: Melo do Nascimento, Larissa (Author) , Terrao, Monica (Author) , Marucha, Kevin (Author) , Liu, Bin (Author) , Falk, Franziska (Author) , Clayton, Christine (Author)
Format: Article (Journal)
Language:English
Published: June 12, 2020
In: The journal of biological chemistry
Year: 2020, Volume: 295, Issue: 32, Pages: 10940-10955
ISSN:1083-351X
DOI:10.1074/jbc.RA120.013306
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1074/jbc.RA120.013306
Verlag, lizenzpflichtig, Volltext: http://www.jbc.org/content/295/32/10940
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Author Notes:Larissa Melo do Nascimento, Monica Terrao, Kevin Kamanyi Marucha, Bin Liu, Franziska Egler, and Christine Clayton

MARC

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520 |a Control of gene expression in kinetoplastids such as trypanosomes depends heavily on RNA-binding proteins that influence mRNA decay and translation. We previously showed that the trypanosome protein MKT1 forms a multicomponent protein complex: MKT1 interacts with PBP1, which in turn recruits LSM12 and poly(A)-binding protein. MKT1 is recruited to mRNAs by sequence-specific RNA-binding proteins, resulting in stabilization of the bound mRNA. We here show that PBP1, LSM12, and a 117-residue protein, XAC1 (Tb927.7.2780), are present in complexes that contain either MKT1 or an MKT1-like protein, MKT1L (Tb927.10.1490). All five proteins are present predominantly in the complexes, and we found evidence for a minor subset of complexes containing both MKT1 and MKT1L. XAC1-containing complexes reproducibly contained RNA-binding proteins that were previously found associated with MKT1. Moreover, XAC1- or MKT1-containing complexes specifically recruited one of the two poly(A)-binding proteins, PABP2, and one of the six cap-binding translation initiation complexes, EIF4E6-EIF4G5. Yeast two-hybrid assay results indicated that MKT1 directly interacts with EIF4G5. MKT1-PBP1 complexes can therefore interact with mRNAs via their poly(A) tails and caps, as well as through sequence-specific RNA-binding proteins. Correspondingly, MKT1 is associated with many mRNAs, although not with those encoding ribosomal proteins. Meanwhile, MKT1L resembles MKT1 at the C terminus but additionally features an N-terminal extension with low-complexity regions. Although MKT1L depletion inhibited cell proliferation, we found no evidence that it specifically interacts with RNA-binding proteins or mRNA. We speculate that MKT1L may compete with MKT1 for PBP1 binding and thereby modulate the function of MKT1-containing complexes. 
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