Increase in Backbone Mobility of the VTS1p-SAM Domain on Binding to SRE–RNA

• Published in: Journal of molecular biology Vol. 396; no. 3; pp. 732 - 746
• Main Authors: Ravindranathan, Sapna, Oberstrass, Florian C., Allain, Frédéric H-.T.
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 26.02.2010
• Subjects: 15N relaxation; Amino Acid Sequence; Base Pairing; Binding Sites; Drosophila; Models, Molecular; Molecular Sequence Data; NMR; Nuclear Magnetic Resonance, Biomolecular; Nucleic Acid Conformation; Protein Binding; Protein Structure, Tertiary; protein–RNA interaction; RNA, Fungal - metabolism; RNA-Binding Proteins - chemistry; RNA-Binding Proteins - metabolism; Saccharomyces cerevisiae - chemistry; Saccharomyces cerevisiae Proteins - chemistry; Saccharomyces cerevisiae Proteins - metabolism; SRE–RNA; VTS1p-SAM domain; NMR; VTS1p-SAM domain; NOE; protein–RNA interaction; SRE; 15N relaxation; SRE–RNA; SAM

The sterile alpha motif (SAM) domain of VTS1p, a posttranscriptional gene regulator, belongs to a family of SAM domains conserved from yeast to humans. Even though SAM domains were originally classified as protein–protein interaction domains, recently, it was shown that the yeast VTS1p-SAM and the S...