An intramolecular disulphide bond in human 4E-T affects its binding to eIF4E1a protein.

ABSTRACT: The cap at the 5'terminus of mRNA is a key determinant of gene expression in eukaryotic cells, which among others is required for cap dependent translation and protects mRNA from degradation. These properties of cap are mediated by several proteins. One of them is 4E-Transporter (4E-T), which plays an important role in translational repression, mRNA decay and P-bodies formation. 4E-T is also one of several proteins that interact with eukaryotic initiation factor 4E (eIF4E), a cap binding protein which is a key component of the translation initiation machinery. The molecular mechanisms underlying the interactions of these two proteins are crucial for mRNA processing. Studying the interactions between human eIF4E1a and the N-terminal fragment of 4E-T that possesses unstructured 4E-binding mo

SUBMITTER: Zuberek J 

PROVIDER: S-EPMC10618305 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature