Abstract
Pyrococcus horikoshii OT3 is a hyperthermophilic archaeaon -isolated from hydrothermal fluid. Because of their genetic features as well as hyperthermophilic properties, macromolecules produced by this thermophilic bacterium have served as an excellent model for structural biology. Ribonuclease P (RNase P) is a ribonucleoprotein complex involved in the processing of the 5′-leader sequence of precursor tRNA (pre-tRNA). We found that RNase P RNA (PhopRNA) and five proteins in P. horikoshii OT3 reconstituted RNase P activity that exhibited enzymatic properties like those of the authentic enzyme. A mutational analysis indicated that nucleotides A40, A41, and U44 in PhopRNA are crucial for catalysis, strongly suggesting that PhopRNA catalyzes the hydrolysis of pre-tRNA in approximately the same manner as eubacterial RNase P RNAs, even though it has no enzymatic activity in the absence of the proteins. The P. horikoshii RNase P proteins are predominantly involved in optimization of PhopRNA's conformation, though individually they are dispensable for RNase P activity in vitro. This chapter summarizes structure-function relationships of the P. horikoshii RNase P subunits, including the high-resolution structural information that is currently available for the protein subunits.
| Original language | English |
|---|---|
| Title of host publication | Microorganisms in Sustainable Agriculture and Biotechnology |
| Publisher | Springer Netherlands |
| Pages | 487-508 |
| Number of pages | 22 |
| Volume | 9789400722149 |
| ISBN (Electronic) | 9789400722149 |
| ISBN (Print) | 9400722133, 9789400722132 |
| DOIs | |
| Publication status | Published - Oct 1 2012 |
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All Science Journal Classification (ASJC) codes
- Immunology and Microbiology(all)
Cite this
Structural biology of the ribonuclease p in the hyperthermophilic archaeon pyrococcus horikoshii OT3. / Kimura, Makoto; Kakuta, Yoshimitsu.
Microorganisms in Sustainable Agriculture and Biotechnology. Vol. 9789400722149 Springer Netherlands, 2012. p. 487-508.Research output: Chapter in Book/Report/Conference proceeding › Chapter
}
TY - CHAP
T1 - Structural biology of the ribonuclease p in the hyperthermophilic archaeon pyrococcus horikoshii OT3
AU - Kimura, Makoto
AU - Kakuta, Yoshimitsu
PY - 2012/10/1
Y1 - 2012/10/1
N2 - Pyrococcus horikoshii OT3 is a hyperthermophilic archaeaon -isolated from hydrothermal fluid. Because of their genetic features as well as hyperthermophilic properties, macromolecules produced by this thermophilic bacterium have served as an excellent model for structural biology. Ribonuclease P (RNase P) is a ribonucleoprotein complex involved in the processing of the 5′-leader sequence of precursor tRNA (pre-tRNA). We found that RNase P RNA (PhopRNA) and five proteins in P. horikoshii OT3 reconstituted RNase P activity that exhibited enzymatic properties like those of the authentic enzyme. A mutational analysis indicated that nucleotides A40, A41, and U44 in PhopRNA are crucial for catalysis, strongly suggesting that PhopRNA catalyzes the hydrolysis of pre-tRNA in approximately the same manner as eubacterial RNase P RNAs, even though it has no enzymatic activity in the absence of the proteins. The P. horikoshii RNase P proteins are predominantly involved in optimization of PhopRNA's conformation, though individually they are dispensable for RNase P activity in vitro. This chapter summarizes structure-function relationships of the P. horikoshii RNase P subunits, including the high-resolution structural information that is currently available for the protein subunits.
AB - Pyrococcus horikoshii OT3 is a hyperthermophilic archaeaon -isolated from hydrothermal fluid. Because of their genetic features as well as hyperthermophilic properties, macromolecules produced by this thermophilic bacterium have served as an excellent model for structural biology. Ribonuclease P (RNase P) is a ribonucleoprotein complex involved in the processing of the 5′-leader sequence of precursor tRNA (pre-tRNA). We found that RNase P RNA (PhopRNA) and five proteins in P. horikoshii OT3 reconstituted RNase P activity that exhibited enzymatic properties like those of the authentic enzyme. A mutational analysis indicated that nucleotides A40, A41, and U44 in PhopRNA are crucial for catalysis, strongly suggesting that PhopRNA catalyzes the hydrolysis of pre-tRNA in approximately the same manner as eubacterial RNase P RNAs, even though it has no enzymatic activity in the absence of the proteins. The P. horikoshii RNase P proteins are predominantly involved in optimization of PhopRNA's conformation, though individually they are dispensable for RNase P activity in vitro. This chapter summarizes structure-function relationships of the P. horikoshii RNase P subunits, including the high-resolution structural information that is currently available for the protein subunits.
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UR - http://www.scopus.com/inward/citedby.url?scp=84906088324&partnerID=8YFLogxK
U2 - 10.1007/978-94-007-2214-9_23
DO - 10.1007/978-94-007-2214-9_23
M3 - Chapter
AN - SCOPUS:84906088324
SN - 9400722133
SN - 9789400722132
VL - 9789400722149
SP - 487
EP - 508
BT - Microorganisms in Sustainable Agriculture and Biotechnology
PB - Springer Netherlands
ER -