A creature with a hundred waggly tails: intrinsically disordered proteins in the ribosome.
Intrinsic disorder (i.e., lack of a unique 3-D structure) is a common phenomenon, and many biologically active proteins are disordered as a whole, or contain long disordered regions. These intrinsically disordered proteins/regions constitute a significant part of all proteomes, and their functional repertoire is complementary to functions of ordered proteins. In fact, intrinsic disorder represents an important driving force for many specific functions. An illustrative example of such disorder-centric functional class is RNA-binding proteins. In this study, we present the results of comprehensive bioinformatics analyses of the abundance and roles of intrinsic disorder in 3,411 ribosomal proteins from 32 species. We show that many ribosomal proteins are intrinsically disordered or hybrid proteins that contain ordered and disordered domains. Predicted globular domains of many ribosomal proteins contain noticeable regions of intrinsic disorder. We also show that disorder in ribosomal proteins has different characteristics compared to other proteins that interact with RNA and DNA including overall abundance, evolutionary conservation, and involvement in protein-protein interactions. Furthermore, intrinsic disorder is not only abundant in the ribosomal proteins, but we demonstrate that it is absolutely necessary for their various functions.
Department of Electrical and Computer Engineering, University of Alberta, Edmonton, AB, T6G 2V4, Canada.
Zhenling
Z
Peng
Christopher J
CJ
Oldfield
Bin
B
Xue
Marcin J
MJ
Mizianty
A Keith
AK
Dunker
Lukasz
L
Kurgan
Vladimir N
VN
Uversky
D000596:Amino Acids / Q000032:analysis; D001105:Archaea / Q000235:genetics; D001419:Bacteria / Q000235:genetics; D019295:Computational Biology; D017124:Conserved Sequence / Q000235:genetics; D030562:Databases, Protein; D056890:Eukaryota / Q000235:genetics; D019143:Evolution, Molecular; D064267:Intrinsically Disordered Proteins / Q000235:genetics* / Q000378:metabolism*; D008958:Models, Molecular; D011487:Protein Conformation; D017434:Protein Structure, Tertiary / Q000235:genetics; D016601:RNA-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000235:genetics / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism*; D013045:Species Specificity
D000596:Amino Acids; D064267:Intrinsically Disordered Proteins; D016601:RNA-Binding Proteins; D012269:Ribosomal Proteins