Proteomics

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The endoplasmic reticulum-associated mRNA-binding protein ERBP1 from Trypanosoma brucei


ABSTRACT: Kinetoplastids rely heavily on post-transcriptional mechanisms for control of gene expression, and on RNA-binding proteins that regulate mRNA splicing, translation and decay. Trypanosoma brucei ERBP1 (Tb927.10.14150) and ERBP2 (Tb927.9.9550) were previously identified as mRNA binding proteins that lack canonical RNA-binding domains. We here show that ERBP1 is associated with the endoplasmic reticulum, like ERBP2, and that the two proteins interact in vivo. Loss of ERBP1 from bloodstream-form T. brucei initially resulted in a growth defect but proliferation was restored after more prolonged cultivation. Results from a pull-down of tagged ERBP1 suggest that it preferentially binds to ribosomal protein mRNAs. The ERBP1 sequence resembles that of Saccharomyces cerevisiae Bfr1, which also localises to the endoplasmic reticulum and binds to ribosomal protein mRNAs. However, unlike Bfr1, ERBP1 does not bind to mRNAs encoding secreted proteins, and it is also not recruited to stress granules after starvation.

INSTRUMENT(S): LTQ Orbitrap Velos, Q Exactive

ORGANISM(S): Trypanosoma Brucei

SUBMITTER: Thomas Ruppert  

LAB HEAD: Thomas Ruppert

PROVIDER: PXD016136 | Pride | 2020-05-27

REPOSITORIES: Pride

Dataset's files

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E-25D165-16-202-03.mgf Mgf
E-25D165-16-202-03.msf Msf
E-25D165-16-202-03.raw Raw
E-25D165-16-202-04.mgf Mgf
E-25D165-16-202-04.msf Msf
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Publications

The endoplasmic reticulum-associated mRNA-binding proteins ERBP1 and ERBP2 interact in bloodstream-form <i>Trypanosoma brucei</i>.

Bajak Kathrin K   Leiss Kevin K   Clayton Christine E CE   Erben Esteban E  

PeerJ 20200214


Kinetoplastids rely heavily on post-transcriptional mechanisms for control of gene expression, and on RNA-binding proteins that regulate mRNA splicing, translation and decay. <i>Trypanosoma brucei</i> ERBP1 (Tb927.10.14150) and ERBP2 (Tb927.9.9550) were previously identified as mRNA binding proteins that lack canonical RNA-binding domains. We show here that ERBP1 is associated with the endoplasmic reticulum, like ERBP2, and that the two proteins interact in vivo. Loss of ERBP1 from bloodstream-f  ...[more]

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