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Brodersen, D.E., Clemons Jr., W.M., Carter, A.P., Wimberly, B.T. and Ramakrishnan, V. (2002) Crystal structure of the 30S ribosomal subunit from Thermus thermophilus: Structure of the proteins and their interactions with 16S RNA. Journal of Molecular Biology, 316, 725- 768. doi:10.1006/jmbi.2001.5359

has been cited by the following article:

• TITLE: Hydrogen bonds are related to the thermal stability of 16S rRNA

  AUTHORS: Hiroshi Nakashima, Ai Fukuoka, Yuka Saitou

  KEYWORDS: Optimal Growth Temperature; 16S Ribosomal RNA; G + C Content; Hydrogen Bonds; Base Pairs; Nucleotide Compositions

  JOURNAL NAME: Journal of Biomedical Science and Engineering, Vol.6 No.1, January 24, 2013

  ABSTRACT: The number of base pairs in the 16S rRNA secondary structures of 51 bacterial sequences was counted, and the number of hydrogen bonds was estimated. The number of hydrogen bonds was highly correlated with the optimal growth temperature (OGT) rather than with the G + C content. Paired and unpaired nucleotides in mesophiles were compared to those in thermophiles. OGT exhibited a relationship with paired nucleotides but not with unpaired nucleotides. The total number of paired as well as unpaired nucleotides in mesophiles was very similar to that in thermophiles. However, the components in base pairs in mesophiles significantly differed from those in thermophiles. As compared with mesophiles, the number of G·C base pairs in thermophiles was high whereas that of A·U base pairs was low. In this study, we showed that hydrogen bonds are important for stabilizing 16S rRNAs at high temperatures.