TY - JOUR
T1 - Yet Another Similarity between Mitochondrial and Bacterial Ribosomal Small Subunit Biogenesis Obtained by Structural Characterization of RbfA from S. aureus
AU - Bikmullin, Aydar G.
AU - Fatkhullin, Bulat
AU - Stetsenko, Artem
AU - Gabdulkhakov, Azat
AU - Garaeva, Natalia
AU - Nurullina, Liliia
AU - Klochkova, Evelina
AU - Golubev, Alexander
AU - Khusainov, Iskander
AU - Trachtmann, Natalie
AU - Blokhin, Dmitriy
AU - Guskov, Albert
AU - Validov, Shamil
AU - Usachev, Konstantin
AU - Yusupov, Marat
PY - 2023/1/20
Y1 - 2023/1/20
N2 - Ribosome biogenesis is a complex and highly accurate conservative process of ribosomal subunit maturation followed by association. Subunit maturation comprises sequential stages of ribosomal RNA and proteins' folding, modification and binding, with the involvement of numerous RNAses, helicases, GTPases, chaperones, RNA, protein-modifying enzymes, and assembly factors. One such assembly factor involved in bacterial 30S subunit maturation is ribosomal binding factor A (RbfA). In this study, we present the crystal (determined at 2.2 Å resolution) and NMR structures of RbfA as well as the 2.9 Å resolution cryo-EM reconstruction of the 30S-RbfA complex from Staphylococcus aureus (S. aureus). Additionally, we show that the manner of RbfA action on the small ribosomal subunit during its maturation is shared between bacteria and mitochondria. The obtained results clarify the function of RbfA in the 30S maturation process and its role in ribosome functioning in general. Furthermore, given that S. aureus is a serious human pathogen, this study provides an additional prospect to develop antimicrobials targeting bacterial pathogens.
AB - Ribosome biogenesis is a complex and highly accurate conservative process of ribosomal subunit maturation followed by association. Subunit maturation comprises sequential stages of ribosomal RNA and proteins' folding, modification and binding, with the involvement of numerous RNAses, helicases, GTPases, chaperones, RNA, protein-modifying enzymes, and assembly factors. One such assembly factor involved in bacterial 30S subunit maturation is ribosomal binding factor A (RbfA). In this study, we present the crystal (determined at 2.2 Å resolution) and NMR structures of RbfA as well as the 2.9 Å resolution cryo-EM reconstruction of the 30S-RbfA complex from Staphylococcus aureus (S. aureus). Additionally, we show that the manner of RbfA action on the small ribosomal subunit during its maturation is shared between bacteria and mitochondria. The obtained results clarify the function of RbfA in the 30S maturation process and its role in ribosome functioning in general. Furthermore, given that S. aureus is a serious human pathogen, this study provides an additional prospect to develop antimicrobials targeting bacterial pathogens.
KW - 30S biogenesis
KW - bacterial ribosomal proteins
KW - RbfA
KW - ribosome
KW - Staphylococcus aureus
KW - translation
UR - http://www.scopus.com/inward/record.url?scp=85147892846&partnerID=8YFLogxK
U2 - 10.3390/ijms24032118
DO - 10.3390/ijms24032118
M3 - Article
C2 - 36768442
AN - SCOPUS:85147892846
SN - 1422-0067
VL - 24
JO - International Journal of Molecular Sciences
JF - International Journal of Molecular Sciences
IS - 3
M1 - 24032118
ER -