Protein-protein interactions in the subunits of ribonuclease P in the hyperthermophilic archaeon Pyrococcus horikoshii OT3.
Ribonuclease P (RNase P) is a ribonucleoprotein complex involved in the processing of the 5' leader sequence of precursor tRNA (pre-tRNA). RNase P in the hyperthermophilic archaeon Pyrococcus horikoshii OT3 consists of RNA and five protein subunits (Ph1481p, Ph1496p, Ph1601p, Ph1771p, and Ph1877p). In vivo interactions among five protein subunits of RNase P in P. horikoshii OT3 were examined using a yeast two-hybrid system. The analysis indicates that proteins Ph1481p and Ph1601p interact strongly with Ph1877p and Ph1771p respectively, whereas Ph1481p interacts moderately with Ph1601p. In contrast, no interaction was detected between Ph1496p and the other four proteins. Co-immunoprecipitation analysis confirmed the interactions obtained by yeast two-hybrid assay.
Laboratory of Biochemistry, Department of Bioscience and Biotechnology, Faculty of Agriculture, Graduate School, Kyushu University, Fukuoka, Japan.
Mayumi
M
Kifusa
Hideo
H
Fukuhara
Takeshi
T
Hayashi
Makoto
M
Kimura
D019843:Archaeal Proteins / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D021122:Protein Subunits; D043902:Pyrococcus horikoshii / Q000201:enzymology*; D043262:Ribonuclease P / Q000737:chemistry* / Q000378:metabolism*; D020798:Two-Hybrid System Techniques
D019843:Archaeal Proteins; D021122:Protein Subunits; D043262:Ribonuclease P