AI Article Synopsis

  • Most transcription in Trypanosoma brucei is polycistronic and relies on post-transcriptional mechanisms for gene expression control, particularly in adapting to various environments.
  • The parasite has multiple isoforms of cap-binding proteins (EIF4E and EIF4G), with EIF4E1 primarily associated with 4E-binding protein 4EIP, which represses translation and destabilizes mRNA.
  • EIF4E1 is not crucial during differentiation between life stages but is necessary for establishing growing forms, while 4EIP is essential during this transition, with some interactions between EIF4E1 and translation initiation factors remaining unclear.

Article Abstract

Most transcription in Trypanosoma brucei is constitutive and polycistronic. Consequently, the parasite relies on post-transcriptional mechanisms, especially affecting translation initiation and mRNA decay, to control gene expression both at steady-state and for adaptation to different environments. The parasite has six isoforms of the cap-binding protein EIF4E as well as five EIF4Gs. EIF4E1 does not bind to any EIF4G, instead being associated with a 4E-binding protein, 4EIP. 4EIP represses translation and reduces the stability of a reporter mRNA when artificially tethered to the 3'-UTR, whether or not EIF4E1 is present. 4EIP is essential during the transition from the mammalian bloodstream form to the procyclic form that lives in the Tsetse vector. In contrast, EIF4E1 is dispensable during differentiation, but is required for establishment of growing procyclic forms. In Leishmania, there is some evidence that EIF4E1 might be active in translation initiation, via direct recruitment of EIF3. However in T. brucei, EIF4E1 showed no detectable association with other translation initiation factors, even in the complete absence of 4EIP. There was some evidence for interactions with NOT complex components, but if these occur they must be weak and transient. We found that EIF4E1is less abundant in the absence of 4EIP, and RNA pull-down results suggested this might occur through co-translational complex assembly. We also report that 4EIP directly recruits the cytosolic terminal uridylyl transferase TUT3 to EIF4E1/4EIP complexes. There was, however, no evidence that TUT3 is essential for 4EIP function.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8608314PMC
http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0258903PLOS

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