Protein recognition of a ribosomal RNA tertiary structure.
Ribosomal protein L11 recognizes a highly conserved, 58 nucleotide domain of large subunit ribosomal RNA. This domain has a set of tertiary interactions that are specifically stabilized by Mg2+ and NH4+ ions. The protein recognizes this tertiary structure, in the sense that ions stabilizing the tertiary structure also promote L11 binding, and a heat stable form of the protein (from Bacillus stearothermophilus) prevents RNA unfolding. We also find that these RNA-binding properties are confined to a approximately 75 amino acid domain of the protein. The larger issue of L11 function within the ribosome is discussed in light of these findings.
Draper
D E
DE
Department of Chemistry, Johns Hopkins University, Baltimore, MD 21218, USA.
Xing
Y
Y
D001426:Bacterial Proteins / Q000378:metabolism; D001483:Base Sequence; D001665:Binding Sites; D001411:Geobacillus stearothermophilus / Q000235:genetics / Q000378:metabolism; D008274:Magnesium / Q000378:metabolism; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D000644:Quaternary Ammonium Compounds / Q000378:metabolism; D012329:RNA, Bacterial / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012335:RNA, Ribosomal / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D012269:Ribosomal Proteins / Q000378:metabolism*
D001426:Bacterial Proteins; D000644:Quaternary Ammonium Compounds; D012329:RNA, Bacterial; D012335:RNA, Ribosomal; D012269:Ribosomal Proteins; C027624:ribosomal protein L11; D008274:Magnesium