Ribonuclease P

1. Front Matter

   Pages i-xiv

   PDF

2. History of RNase P and Overview of Its Catalytic Activity

   • Sidney Altman

   Pages 1-15

3. The Evolution of RNase P and Its RNA

   • J. Christopher Ellis, James W. Brown

   Pages 17-40

4. Over a Decade of Bacterial Ribonuclease P Modeling

   • Benoît Masquida, Fabrice Jossinet, Eric Westhof

   Pages 41-62

5. Structural Studies of Ribonuclease P

   • Alfonso Mondragón

   Pages 63-78

6. Folding of Bacterial RNase P RNA

   • Tao Pan

   Pages 79-91

7. Kinetic Mechanism of Bacterial RNase P

   • Kristin S. Koutmou, John Hsieh, Carol A. Fierke

   Pages 93-111

8. Roles of Metal Ions in RNase P Catalysis

   • Leif A. Kirsebom

   Pages 113-134

9. Challenges in RNase P Substrate Recognition: Considering the Biological Context

   • Michael Harris, Lindsay Yandek

   Pages 135-151

10. Archaeal RNase P: A Mosaic of Its Bacterial and Eukaryal Relatives

    • Lien B. Lai, I-Ming Cho, Wen-Yi Chen, Venkat Gopalan

    Pages 153-172

11. Eukaryote RNase P and RNase MRP

    • Scott C. Walker, Michael C. Marvin, David R. Engelke

    Pages 173-202

12. RNase P from Organelles

    • Agustín Vioque

    Pages 203-222

13. Human RNase P and Transcription

    • Nayef Jarrous, Robert Reiner, Yana Dehtiar

    Pages 223-234

14. RNase P as a Drug Target

    • Dagmar K. Willkomm, Patrick Pfeffer, Klaus Reuter, Gerhard Klebe, Roland K. Hartmann

    Pages 235-256

15. Ribonuclease P as a Tool

    • Fenyong Liu

    Pages 257-275

16. Back Matter

    Pages 227-283

    PDF

The Discovery of Ribonuclease P and Enzymatic Activity of Its RNA Subunit Sydney Brenner and Francis H. C. Crick had a specific project in mind when they offered Sidney Altman a position in their group in 1969 to conduct postdoctoral research at the Medical Research Council Laboratory of Molecular Biology (LMB) in Cambridge, England. At the time, an intense international competition was on- ing in as many as a dozen labs to determine the three-dimensional structure of tRNA. At the LMB, Aaron Klug was attacking the structure by crystallographic analysis with Brian F. C. Clark providing large amounts of purified phenylalanine tRNA. (Eventually, Aaron announced his empirically determined 3-D structure of yeast phenylalanine tRNA, a structure that is generally common to tRNAs, due in part to several conserved, novel three-way nucleotide interactions. ) Concurrently, Michael Levitt, a Ph. D. student of Francis, was visually scrutinizing the cloverleaf secondary structure of the 14 tRNA sequences known at the time. Levitt was searching for nucleotide covariation in different parts of the molecules that were conserved in the 14 sequences known at the time. He identified a possible covariation of an apparent Watson-Crick pairing type between the residues at position 15 from the 5’ end of the tRNA and residue 48. This association implied these parts of the tRNA, namely the D loop containing residue 15 and the 5’ end of the T stem-adjoining residue 48, folded on one another in a tertiary structure shared by different tRNAs.

• RNA
• biochemistry
• enzymes
• liu
• ribonuclease
• rnase p
• transcription
• translation
• Proteomics

• School of Public Health, University of California, Berkeley, Berkeley, U.S.A.

  Fenyong Liu

• Dept. Molecular, Cellular &, Yale University, New Haven, U.S.A.

  Sidney Altman

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