YbxF, a Protein Associated with Exponential-Phase Ribosomes in Bacillus subtilis-Reference-Cited by-同舟云学术

YbxF, a Protein Associated with Exponential-Phase Ribosomes in Bacillus subtilis

Published:2007-07 Issue:13 Volume:189 Page:4809-4814
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

Sojka Luděk¹²,Fučík Vladimír¹³,Krásný Libor¹²,Barvík Ivan⁴,Jonák Jiří¹²⁵

Affiliation:

1. Department of Bacteriology, Institute of Molecular Genetics ASCR, Vídeňská 1083, 142 20 Prague 4, Czech Republic

2. Laboratory of Molecular Genetics of Bacteria, Institute of Microbiology ASCR, Vídeňská 1083, 142 20 Prague 4, Czech Republic

3. Department of Natural Compounds, Institute of Organic Chemistry and Biochemistry ASCR, Flemingovo nám. 2, 16610 Prague 6, Czech Republic

4. Institute of Physics, Faculty of Mathematics and Physics, Charles University, Ke Karlovu 5, 121 16 Prague 2, Czech Republic

5. Institute of Medical Biochemistry, First Medical Faculty, Charles University, Kateřinská 32, 12108 Prague 2, Czech Republic

Abstract

ABSTRACT The ybxF gene is a member of the streptomycin operon in a wide range of gram-positive bacteria. In Bacillus subtilis , it codes for a small basic protein (82 amino acids, pI 9.51) of unknown function. We demonstrate that, in B. subtilis , YbxF localizes to the ribosome, primarily to the 50S subunit, with dependence on growth phase. Based on three-dimensional structures of YbxF generated by homology modeling, we identified helix 2 as important for the interaction with the ribosome. Subsequent mutational analysis of helix 2 revealed Lys24 as crucial for the interaction. Neither the B. subtilis ybxF gene nor its paralogue, the ymxC gene, is essential, as shown by probing Δ ybxF , Δ ymxC , or Δ ybxF Δ ymxC double deletion strains in several functional assays.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/JB.01786-06

Reference27 articles.

1. Anagnostopoulos, C., and J. Spizizen. 1960. Requirements for transformation in Bacillus subtilis. J. Bacteriol. 81 : 741-746.

2. Arndt, E., T. Scholzen, W. Kromer, T. Hatakeyama, and M. Kimura. 1991. Primary structures of ribosomal proteins from the archaebacterium Halobacterium marismortui and the eubacterium Bacillus stearothermophilus. Biochimie 73 : 657-668.

3. Ban, N., P. Nissen, J. Hansen, P. B. Moore, and T. A. Steitz. 2000. The complete atomic structure of the large ribosomal subunit at 2.4 A resolution. Science 289 : 905-920.

4. Chao, J. A., G. S. Prasad, S. A. White, C. D. Stout, and J. R. Williamson. 2003. Inherent protein structural flexibility at the RNA-binding interface of L30e. J. Mol. Biol. 326 : 999-1004.

5. Charron, C., X. Manival, B. Charpentier, C. Branlant, and A. Aubry. 2004. Purification, crystallization and preliminary X-ray diffraction data of L7Ae sRNP core protein from Pyrococcus abyssii. Acta Crystallogr. D 60 : 122-124.

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