TY - JOUR
T1 - Crystal structure and functional analysis of an archaeal chromatin protein alba from the hyperthermophilic archaeon Pyrococcus horikoshii OT3
AU - Hada, Kazumasa
AU - Nakashima, Takashi
AU - Osawa, Takuo
AU - Shimada, Hiroaki
AU - Kakuta, Yoshimitsu
AU - Kimura, Makoto
N1 - Funding Information:
using synchrotron radiation at beamlines. This work was supported in part by a grant from the National Project on Protein Structural and Functional Analysis from the Ministry of Education, Culture, Sports, Science, and Technology of Japan.
PY - 2008
Y1 - 2008
N2 - The crystal structure of the Alba protein (PhoAlba) from a hyperthermophilic archaeon, Pyrococcus horikoshii OT3, was determined at a resolution of 2.8 Å. PhoAlba structurally belongs to the α/β proteins and is similar not only to archaeal homologues but also to RNA-binding proteins, including the C-terminal half of initiation factor 3 (IF3-C) from Bacillus stearothermophilus, an Esherichia coli protein implicated in cell division (Yhhp), and an Arabidopsis protein of unknown function. We found by gel shift assay that PhoAlba interacts with both ribonuclease P (RNase P) RNA (PhopRNA) and precursor-tRNATyr (pre-tRNATyr) in P. horikoshii. However, the addition of PhoAlba to reconstituted particles composed of PhopRNA and four or five protein subunits had little influence on either the pre-tRNA processing activity or the optimum temperature for the processing activity. These results suggest that PhoAlba contributes little to the catalytic activity of P. horikoshii RNase P.
AB - The crystal structure of the Alba protein (PhoAlba) from a hyperthermophilic archaeon, Pyrococcus horikoshii OT3, was determined at a resolution of 2.8 Å. PhoAlba structurally belongs to the α/β proteins and is similar not only to archaeal homologues but also to RNA-binding proteins, including the C-terminal half of initiation factor 3 (IF3-C) from Bacillus stearothermophilus, an Esherichia coli protein implicated in cell division (Yhhp), and an Arabidopsis protein of unknown function. We found by gel shift assay that PhoAlba interacts with both ribonuclease P (RNase P) RNA (PhopRNA) and precursor-tRNATyr (pre-tRNATyr) in P. horikoshii. However, the addition of PhoAlba to reconstituted particles composed of PhopRNA and four or five protein subunits had little influence on either the pre-tRNA processing activity or the optimum temperature for the processing activity. These results suggest that PhoAlba contributes little to the catalytic activity of P. horikoshii RNase P.
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U2 - 10.1271/bbb.70639
DO - 10.1271/bbb.70639
M3 - Article
C2 - 18323660
AN - SCOPUS:41549128121
SN - 0916-8451
VL - 72
SP - 749
EP - 758
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
IS - 3
ER -