title: Functional role of ribosomal signatures.
abstract: Although structure and sequence signatures in ribosomal RNA and proteins are defining characteristics of the three domains of life and instrumental in constructing the modern phylogeny, little is known about their functional roles in the ribosome. In this work, the largest coevolving RNA/protein signatures in the bacterial 30S ribosome are investigated both experimentally and computationally through all-atom molecular-dynamics simulations. The complex includes the N-terminal fragment of the ribosomal protein S4, which is a primary binding protein that initiates 30S small subunit assembly from the 5' domain, and helix 16 (h16), which is part of the five-way junction in 16S rRNA. Our results show that the S4 N-terminus signature is intrinsically disordered in solution, whereas h16 is relatively stable by itself. The dynamic disordered property of the protein is exploited to couple the folding and binding process to the five-way junction, and the results provide insight into the mechanism for the early and fast binding of S4 in the assembly of the ribosomal small subunit.
authors.affiliation: Center for Biophysics and Computational Biology, Department of Chemistry, University of Illinois, Urbana, Illinois, USA.
authors.forename: Ke
authors.initials: K
authors.lastname: Chen
authors.forename: John
authors.initials: J
authors.lastname: Eargle
authors.forename: Krishnarjun
authors.initials: K
authors.lastname: Sarkar
authors.forename: Martin
authors.initials: M
authors.lastname: Gruebele
authors.forename: Zaida
authors.initials: Z
authors.lastname: Luthey-Schulten
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D003198:Computer Simulation; D004926:Escherichia coli / Q000378:metabolism*; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D018583:Pliability; D011485:Protein Binding; D055550:Protein Stability; D017433:Protein Structure, Secondary; D058767:Protein Unfolding; D012336:RNA, Ribosomal, 16S / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012269:Ribosomal Proteins / Q000737:chemistry / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism*; D013696:Temperature
chemical_list: D012336:RNA, Ribosomal, 16S; D012269:Ribosomal Proteins; C031798:ribosomal protein S4