Multiple Puf proteins regulate the stability of ribosome biogenesis transcripts

Fischer, Anthony D.; Olivas, Wendy M.

doi:10.1080/15476286.2018.1521211

Cited by 16 publications

(12 citation statements)

References 85 publications

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“…RNA-binding proteins have been shown to be important in ribosome biogenesis and development [54,55,56,57]. Puf6 and Loc1 have been shown to regulate the cellular distribution of ASH1 mRNA.…”

Section: Discussionmentioning

confidence: 99%

Puf6 and Loc1 Are the Dedicated Chaperones of Ribosomal Protein Rpl43 in Saccharomyces cerevisiae

Liang

Yueh

Hsu

et al. 2019

IJMS

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Ribosomal proteins are highly expressed, and the quality of ribosomal proteins must be rigorously controlled to build up a functional ribosome. Rpl43, ribosomal protein large subunit 43, is located nearby the E-site of ribosomes. In our previous study, we found that Puf6, Loc1, and Rpl43 form a trimeric complex in Saccharomyces cerevisiae. Rpl43 protein levels are under-accumulated in the absence of PUF6 or LOC1. However, why the loss of Puf6 or Loc1 decreased the protein levels of Rpl43 remained unclear. In the present study, we further dissected the connections among these three proteins and found that the processing defects of pre-ribosomal RNA in puf6Δ and loc1Δ are similar to those of the mutant with depletion of Rpl43. The stability of newly synthesized Rpl43 protein decreased slightly in puf6Δ and significantly in loc1Δ. We also found that Puf6 and Loc1 could interact with nascent Rpl43 co-translationally via the N-terminus of Rpl43. While the association and dissociation of Rpl43 with karyopherins did not depend on Puf6 and Loc1, Puf6 and Loc1 interacted with nascent Rpl43 in collaboration. While the N-terminus of Puf6 contained nuclear localization signals for transport, the PUF (Pumilio) domain was essential to interaction with Loc1, Rpl43, and 60S subunits. The C-terminus of Loc1 is more important for interaction with Puf6 and Rpl43. In this study, we found that Puf6 and Loc1 are the dedicated chaperones of ribosomal protein Rpl43 and also analyzed the potential interaction domains among the three proteins. Correct formation of the Puf6, Loc1, and Rpl43 ternary complex is required to properly proceed to the next step in 60S biogenesis.

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Section: Discussionmentioning

confidence: 99%

Puf6 and Loc1 Are the Dedicated Chaperones of Ribosomal Protein Rpl43 in Saccharomyces cerevisiae

Liang

Yueh

Hsu

et al. 2019

IJMS

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“…We suggest, therefore, that the functions of PUF3 can be taken over by overproduction, or perhaps altered modification, of another protein -most likely, another member of the PUF family. This would not be unusual -the functions of Puf proteins also overlap in Saccharomyces cerevisiae [6]. In T. brucei, the most closely related proteins to PUF3 are PUF1 and PUF4 (S1 Fig, Fig 7).…”

Section: Discussionmentioning

confidence: 92%

Expression of normal levels of the Pumilio domain protein PUF3 is required for optimal growth of Trypanosoma brucei

Marucha

Clayton

2019

Preprint

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The Trypanosoma brucei pumilio domain protein PUF3 is a cytosolic mRNA-binding protein that suppresses expression when tethered to a reporter mRNA. PUF3 was not essential in bloodstream-form or procyclic-form trypanosomes, and RNAi in bloodstream forms had no significant effect on the transcriptome. There was little evidence for specific binding of PUF3 to bloodstream-form mRNAs and mass spectrometry revealed no binding partners that might explain its suppressive activity. Ectopic expression of Cterminally tagged PUF3 in procyclic forms impaired viability. Reduction of PUF3 in bloodstream forms caused a slight growth defect and slightly delayed differentiation to the procyclic form, but the cells lost both defects upon prolonged cultivation. Procyclic forms without PUF3 grew somewhat slower than wild-type, but were able to transform to bloodstream forms after induced expression of the bloodstream-form RNA-binding protein RBP10. We suggest that PUF3 is implicated in fine-tuning gene expression. Since PUF3 is present throughout the Kinetoplastida, selection for its retention may occur within the arthropod vector.

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“…In other organisms, also, Pumilio domain proteins tend to be needed in order to fine-tune gene expression, rather than to effect big changes. Indeed, laboratory yeast that lacks all five cytosolic mRNA-binding Pumilio domain proteins is still viable (Fischer and Olivas, 2018).…”

Section: Discussionmentioning

confidence: 99%

“…We suggest, therefore, that the functions of PUF3 can be taken over by changes in the levels of, or altered modification of, another protein – most likely, another member of the PUF family. This would not be unusual: the functions of Puf proteins also overlap in Saccharomyces cerevisiae (Fischer and Olivas, 2018). In T. brucei , the most closely related proteins to PUF3 are PUF1 and PUF4 (Figs 1 and 2A).…”

Section: Discussionmentioning

confidence: 99%

Roles of the Pumilio domain protein PUF3 inTrypanosoma bruceigrowth and differentiation

Marucha¹,

Clayton²

2020

Parasitology

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Trypanosomes strongly rely on post-transcriptional mechanisms to control gene expression. Several Opisthokont Pumilio domain proteins are known to suppress expression when bound to mRNAs. The Trypanosoma brucei Pumilio domain protein PUF3 is a cytosolic mRNA-binding protein that suppresses expression when tethered to a reporter mRNA. RNA-binding studies showed that PUF3 preferentially binds to mRNAs with a classical Pumilio-domain recognition motif, UGUA[U/C]AUU. RNA-interference-mediated reduction of PUF3 in bloodstream forms caused a minor growth defect, but the transcriptome was not affected. Depletion of PUF3 also slightly delayed differentiation to the procyclic form. However, both PUF3 genes could be deleted in cultured bloodstream- and procyclic-form trypanosomes. Procyclic forms without PUF3 also grew somewhat slower than wild-type, but ectopic expression of C-terminally tagged PUF3 impaired their viability. PUF3 was not required for RBP10-induced differentiation of procyclic forms to bloodstream forms. Mass spectrometry revealed no PUF3 binding partners that might explain its suppressive activity. We conclude that PUF3 may have a role in fine-tuning gene expression. Since PUF3 is conserved in all Kinetoplastids, including those that do not infect vertebrates, we suggest that it might confer advantages within the invertebrate host.

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Multiple Puf proteins regulate the stability of ribosome biogenesis transcripts

Cited by 16 publications

References 85 publications

Puf6 and Loc1 Are the Dedicated Chaperones of Ribosomal Protein Rpl43 in Saccharomyces cerevisiae

Puf6 and Loc1 Are the Dedicated Chaperones of Ribosomal Protein Rpl43 in Saccharomyces cerevisiae

Expression of normal levels of the Pumilio domain protein PUF3 is required for optimal growth of Trypanosoma brucei

Roles of the Pumilio domain protein PUF3 inTrypanosoma bruceigrowth and differentiation

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