Next Article in Journal
Human Fibrinogen: Molecular and Genetic Aspects of Congenital Disorders
Next Article in Special Issue
The Cyanobacterial Ribosomal-Associated Protein LrtA from Synechocystis sp. PCC 6803 Is an Oligomeric Protein in Solution with Chameleonic Sequence Properties
Previous Article in Journal
Candidate Genes for Yellow Leaf Color in Common Wheat (Triticum aestivum L.) and Major Related Metabolic Pathways according to Transcriptome Profiling
Previous Article in Special Issue
Acetylation Disfavors Tau Phase Separation
Open AccessArticle

Deciphering RNA-Recognition Patterns of Intrinsically Disordered Proteins

Department of Biotechnology, Bhupat and Jyoti Mehta School of Biosciences, Indian Institute of Technology Madras, Chennai 600 036, Tamilnadu, India
School of Computational and Integrative Sciences, Jawaharlal Nehru University, New Delhi 110 067, India
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2018, 19(6), 1595;
Received: 12 April 2018 / Revised: 10 May 2018 / Accepted: 16 May 2018 / Published: 29 May 2018
Intrinsically disordered regions (IDRs) and protein (IDPs) are highly flexible owing to their lack of well-defined structures. A subset of such proteins interacts with various substrates; including RNA; frequently adopting regular structures in the final complex. In this work; we have analysed a dataset of protein–RNA complexes undergoing disorder-to-order transition (DOT) upon binding. We found that DOT regions are generally small in size (less than 3 residues) for RNA binding proteins. Like structured proteins; positively charged residues are found to interact with RNA molecules; indicating the dominance of electrostatic and cation-π interactions. However, a comparison of binding frequency shows that interface hydrophobic and aromatic residues have more interactions in only DOT regions than in a protein. Further; DOT regions have significantly higher exposure to water than their structured counterparts. Interactions of DOT regions with RNA increase the sheet formation with minor changes in helix forming residues. We have computed the interaction energy for amino acids–nucleotide pairs; which showed the preference of His–G; Asn–U and Ser–U at for the interface of DOT regions. This study provides insights to understand protein–RNA interactions and the results could also be used for developing a tool for identifying DOT regions in RNA binding proteins. View Full-Text
Keywords: intrinsically disorder proteins; disorder-to-order regions; protein–RNA interactions; unstructured proteins intrinsically disorder proteins; disorder-to-order regions; protein–RNA interactions; unstructured proteins
Show Figures

Graphical abstract

MDPI and ACS Style

Srivastava, A.; Ahmad, S.; Gromiha, M.M. Deciphering RNA-Recognition Patterns of Intrinsically Disordered Proteins. Int. J. Mol. Sci. 2018, 19, 1595.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

Back to TopTop