Assembly of an active translation initiation factor complex by a viral protein

Article Abstract:

A study is presented to establish that the herpes simplex virus-1 (HSV-1) ICP6 polypeptide associates with eIF4G, the cap-binding protein, to promote eIF4F complex assembly. The factors which are capable of interacting with eIF4G and promoting eIF4G complex assembly may play important roles in a variety of processes where translation complexes need to be remodeled or assembled on populations of newly synthesized or derepressed mRNAs.

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Site-specific phosphorylation of a checkpoint mediator protein controls its responses to different DNA structures

Article Abstract:

The checkpoint mediator protein Claspin is indespensable for the ATR-dependent phosphorylation of Chk1 in response to stalled DNA replication forks in Xenopus egg extracts. Site-specific phosphorylation of a checkpoint mediator protein is a crucial determinant in the discrimination between various checkpoint-inducing structures.

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Phosphorylation of eIF4E by Mnk-1 enhances HSV-1 translation and replication in quiscent cells.

Article Abstract:

A study on contribution of translation initiation factor, eIF4E, phosphorylation in herpes simplex virus-1(HSV-1) growth is conducted. The results reveal that phosphorylation of eIF4E by mnk-1 is critical for viral protein synthesis and replication.

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