RNA-binding proteins: modular design for efficient function

Abstract

Many RNA-binding proteins have modular structures, being composed of multiple repeats of just a few basic domains that are arranged in a variety of ways to satisfy their diverse functional requirements. Recent studies have investigated how different modules cooperate in regulating the RNA binding specificity and the biological activity of these proteins. They have also investigated how multiple modules cooperate with enzymatic domains to regulate the catalytic activity of enzymes acting upon RNA. These studies have shown how multiple modules define, for many RNA-binding proteins, the fundamental structural unit that is responsible for their biological function.

Towards deciphering the principles underlying an mRNA recognition code

“…This review analyzes recently published structural data (spanning 2006-2007) on specific mRNA recognition events, and complements excellent earlier reviews on protein-RNA [2][3][4][5] and metabolite-mRNA [6][7][8] recognition.…”

The human RBPome: From genes and proteins to human disease

“…The heterogeneity in the functions of these proteins is due to the presence of different RNA binding domains that recognize RNA. RBPs are built with multiple copies of a unique domain or a mosaic of different domains that confer specificity and affinity [29]. Hence, identifying the presence of various domains can provide clues to novel functions of RBPs.…”

Picornavirus IRES elements: RNA structure and host protein interactions

“…Given the ability of RBPs to recognize multiple targets (reviewed in Lunde et al, 2007), it is not surprising that secondary protein-protein or RNA-protein bridges could facilitate IRES activity. An illustrative example of a functional protein-protein bridge is provided by the splicing factor SRp20 ( Fig.…”