TY - JOUR
T1 - Crystallization and preliminary X-ray crystallographic analysis of ribosome assembly factors
T2 - The Rpf2-Rrs1 complex
AU - Asano, Nozomi
AU - Nakamura, Akiyoshi
AU - Komoda, Keisuke
AU - Kato, Koji
AU - Tanaka, Isao
AU - Yao, Min
N1 - Publisher Copyright:
© 2014 International Unoin of Crystallography.
PY - 2014/12/1
Y1 - 2014/12/1
N2 - Rpf2 and Rrs1 are essential proteins for ribosome biogenesis. These proteins form a complex (the Rpf2-subcomplex) with 5S rRNA and two ribosomal proteins (L5 and L11). This complex is recruited to the ribosome precursor (the 90S pre-ribosome). This recruitment is necessary for the maturation of 25S rRNA. Genetic depletion of Rpf2 and Rrs1 results in accumulation of the 25S rRNA precursor. In this study, Rpf2 and Rrs1 from Aspergillus nidulans were co-overexpressed in Escherichia coli, purified and crystallized. Subsequent analysis revealed that these crystals contained the central core region of the complex consisting of both N-terminal domains. X-ray diffraction data were collected to 2.35Å resolution. Preliminary analysis revealed that the crystals belonged to space group P212121, with unit-cell parameters a = 54.1, b = 123.3, c = 133.8Å. There are two complexes in the asymmetric unit. Structure determination using selenomethionine-labelled protein is in progress.
AB - Rpf2 and Rrs1 are essential proteins for ribosome biogenesis. These proteins form a complex (the Rpf2-subcomplex) with 5S rRNA and two ribosomal proteins (L5 and L11). This complex is recruited to the ribosome precursor (the 90S pre-ribosome). This recruitment is necessary for the maturation of 25S rRNA. Genetic depletion of Rpf2 and Rrs1 results in accumulation of the 25S rRNA precursor. In this study, Rpf2 and Rrs1 from Aspergillus nidulans were co-overexpressed in Escherichia coli, purified and crystallized. Subsequent analysis revealed that these crystals contained the central core region of the complex consisting of both N-terminal domains. X-ray diffraction data were collected to 2.35Å resolution. Preliminary analysis revealed that the crystals belonged to space group P212121, with unit-cell parameters a = 54.1, b = 123.3, c = 133.8Å. There are two complexes in the asymmetric unit. Structure determination using selenomethionine-labelled protein is in progress.
KW - Aspergillus nidulans
KW - Rpf2
KW - Rrs1
KW - ribosome assembly factors
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U2 - 10.1107/S2053230X14024182
DO - 10.1107/S2053230X14024182
M3 - Article
C2 - 25484219
AN - SCOPUS:84925884550
SN - 1744-3091
VL - 70
SP - 1649
EP - 1652
JO - Acta Crystallographica Section F:Structural Biology Communications
JF - Acta Crystallographica Section F:Structural Biology Communications
ER -