On archaeal homologs of the human RNase P proteins Pop5 and Rpp30 in the hyperthermophilic archaeon Thermococcus kodakarensis
| Autor: | Kotaro Suematsu, Toshifumi Ueda, Yoshimitsu Kakuta, Makoto Kimura, Takashi Nakashima |
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| Rok vydání: | 2015 |
| Předmět: |
Models
Molecular RNase P Molecular Sequence Data Crystallography X-Ray Cleavage (embryo) Autoantigens Applied Microbiology and Biotechnology Biochemistry RNase PH Protein Structure Secondary Ribonuclease P Analytical Chemistry Pyrococcus horikoshii Hydrolase TIM barrel Homologous chromosome Humans Amino Acid Sequence Molecular Biology Conserved Sequence Sequence Homology Amino Acid biology Organic Chemistry General Medicine biology.organism_classification Thermococcus kodakarensis Thermococcus Biotechnology |
| Zdroj: | Bioscience, Biotechnology, and Biochemistry. 79:952-959 |
| ISSN: | 1347-6947 0916-8451 |
| DOI: | 10.1080/09168451.2014.1003130 |
| Popis: | The ribonuclease P (RNase P) proteins TkoPop5 and TkoRpp30, homologs of human Pop5 and Rpp30, respectively, in the hyperthermophilic archaeon Thermococcus kodakarensis were prepared and characterized with respect to pre-tRNA cleavage activity using the reconstitution system of the well-studied Pyrococcus horikoshii RNase P. The reconstituted particle containing TkoPop5 in place of the P. horikoshii counterpart PhoPop5 retained pre-tRNA cleavage activity comparable to that of the reconstituted P. horikoshii RNase P, while that containing TkoRpp30 instead of its corresponding protein PhoRpp30 had slightly lower activity than the P. horikoshii RNase P. Moreover, we determined crystal structures of TkoRpp30 alone and in complex with TkoPop5. Like their P. horikoshii counterparts, whose structures were solved previously, TkoRpp30 and TkoPop5 fold into TIM barrel and RRM-like fold, respectively. This finding demonstrates that RNase P proteins in T. kodakarensis and P. horikoshii are interchangeable and that their three-dimensional structures are highly conserved. |
| Databáze: | OpenAIRE |
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