A divergent Pumilio repeat protein family for pre-rRNA processing and mRNA localization

作者：Qiu Chen; McCann Kathleen L; Wine Robert N; Baserga Susan J^*; Hall Traci M Tanaka

来源：Proceedings of the National Academy of Sciences of the United States of America, 2014, 111(52): 18554-18559.

DOI：10.1073/pnas.1407634112

• Puf-A
• crystal structure
• Puf6
• ribosome biogenesis
• mRNA localization

Pumilio/feminization of XX and XO animals (fem)-3 mRNA-binding factor (PUF) proteins bind sequence specifically to mRNA targets using a single-stranded RNA-binding domain comprising eight Pumilio (PUM) repeats. PUM repeats have now been identified in proteins that function in pre-rRNA processing, including human Puf-A and yeast Puf6. This is a role not previously ascribed to PUF proteins. Here we present crystal structures of human Puf-A that reveal a class of nucleic acid-binding proteins with 11 PUM repeats arranged in an "L"-like shape. In contrast to classical PUF proteins, Puf-A forms sequence-independent interactions with DNA or RNA, mediated by conserved basic residues. We demonstrate that equivalent basic residues in yeast Puf6 are important for RNA binding, pre-rRNA processing, and mRNA localization. Thus, PUM repeats can be assembled into alternative folds that bind to structured nucleic acids in addition to forming canonical eight-repeat crescent-shaped RNA-binding domains found in classical PUF proteins.

• 出版日期2014-12-30
• 单位NIH