Abstract
The zinc finger proteins make up a significant part of the proteome and perform a huge variety of functions in the cell. The CCCH-type zinc finger proteins have gained attention due to their unusual ability to interact with RNA and thereby control different steps of RNA metabolism. Since virus infections interfere with RNA metabolism, dynamic changes in the CCCH-type zinc finger proteins and virus replication are expected to happen. In the present review, we will discuss how three CCCH-type zinc finger proteins, ZC3H11A, MKRN1, and U2AF1, interfere with human adenovirus replication. We will summarize the functions of these three cellular proteins and focus on their potential pro- or anti-viral activities during a lytic human adenovirus infection.
Highlights
This study showed that amyotrophic lateral sclerosis (ALS)-linked mutations increase Matrin-3 co-localization with the TREX complex components, which may explain the nuclear mRNA export defects in ALS patients [69]
The CCCH-type zinc finger (ZnF) proteins have emerged as the essential regulators of RNA metabolism
Even if most Human adenoviruses (HAdVs) infections are self-limiting, fatal infections can occur in immuno-compromised hosts and occasionally in healthy children and adults infected with particular HAdV types (e.g., HAdV-7) [88,89]
Summary
Zinc finger proteins are a big family of proteins with characteristic zinc finger (ZnF) domains present in the protein sequence. The Xenopus laevis transcription factor TFIIIA has played a key role in understanding ZnF structures This essential protein contains nine consecutive, 30 amino acid long sequence motifs, which fold around zinc ions and form a structure that visually resembles a “finger”, the name zinc finger [2,3]. The cysteine (C) and histidine (H) residues are important for the ZnF motifs and coordinate the zinc ions and thereby stabilize the ZnF structure. A classic example here is the TFIIIA ZnF motif, where the zinc ion is maintained by two cysteine and two histidine residues (C2 H2 ). Substitutions of the zinc coordinating histidine residues within the ZnF motifs inhibit TFIIIA function as a transcription factor [4,5]. The ZnF domains appear to be multifunctional since in addition to binding to nucleic acids, they can mediate multiple protein-protein interactions and recognize a variety of post-translational modification [15,16]
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