Open Access
Molecular and Cellular Biology, volume 28, issue 10, pages 3151-3161
Bud23 Methylates G1575 of 18S rRNA and Is Required for Efficient Nuclear Export of Pre-40S Subunits
White Joshua
1
,
Li Zhihua
2
,
Sardana Richa
1
,
Bujnicki Janusz M.
3, 4
,
Marcotte Edward M.
2
,
Johnson Arlen W
1
1
Section of Molecular Genetics and Microbiology, Institute for Cellular and Molecular Biology
2
Center for Systems and Synthetic Biology, Department of Chemistry and Biochemistry, The University of Texas at Austin, Austin, Texas 78712
|
3
Bioinformatics Laboratory, Institute of Molecular Biology and Biotechnology, Adam Mickiewicz University, Umultowska 89, PL-61-614 Poznan, Poland
|
4
Laboratory of Bioinformatics and Protein Engineering, International Institute of Molecular and Cell Biology, Trojdena 4, PL-02-109 Warsaw, Poland
|
Publication type: Journal Article
Publication date: 2008-05-15
Journal:
Molecular and Cellular Biology
Quartile SCImago
Q1
Quartile WOS
Q2
Impact factor: 5.3
ISSN: 02707306, 10985549
PubMed ID:
18332120
Molecular Biology
Cell Biology
Abstract
ABSTRACT BUD23 was identified from a bioinformatics analysis of Saccharomyces cerevisiae genes involved in ribosome biogenesis. Deletion of BUD23 leads to severely impaired growth, reduced levels of the small (40S) ribosomal subunit, and a block in processing 20S rRNA to 18S rRNA, a late step in 40S maturation. Bud23 belongs to the S-adenosylmethionine-dependent Rossmann-fold methyltransferase superfamily and is related to small-molecule methyltransferases. Nevertheless, we considered that Bud23 methylates rRNA. Methylation of G1575 is the only mapped modification for which the methylase has not been assigned. Here, we show that this modification is lost in bud23 mutants. The nuclear accumulation of the small-subunit reporters Rps2-green fluorescent protein (GFP) and Rps3-GFP, as well as the rRNA processing intermediate, the 5′ internal transcribed spacer 1, indicate that bud23 mutants are defective for small-subunit export. Mutations in Bud23 that inactivated its methyltransferase activity complemented a bud23Δ mutant. In addition, mutant ribosomes in which G1575 was changed to adenosine supported growth comparable to that of cells with wild-type ribosomes. Thus, Bud23 protein, but not its methyltransferase activity, is important for biogenesis and export of the 40S subunit in yeast.
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- We do not take into account publications that without a DOI.
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GOST
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White J. et al. Bud23 Methylates G1575 of 18S rRNA and Is Required for Efficient Nuclear Export of Pre-40S Subunits // Molecular and Cellular Biology. 2008. Vol. 28. No. 10. pp. 3151-3161.
GOST all authors (up to 50)
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White J., Li Z., Sardana R., Bujnicki J. M., Marcotte E. M., Johnson A. W. Bud23 Methylates G1575 of 18S rRNA and Is Required for Efficient Nuclear Export of Pre-40S Subunits // Molecular and Cellular Biology. 2008. Vol. 28. No. 10. pp. 3151-3161.
Cite this
RIS
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TY - JOUR
DO - 10.1128/MCB.01674-07
UR - https://doi.org/10.1128%2FMCB.01674-07
TI - Bud23 Methylates G1575 of 18S rRNA and Is Required for Efficient Nuclear Export of Pre-40S Subunits
T2 - Molecular and Cellular Biology
AU - White, Joshua
AU - Sardana, Richa
AU - Bujnicki, Janusz M.
AU - Marcotte, Edward M.
AU - Johnson, Arlen W
AU - Li, Zhihua
PY - 2008
DA - 2008/05/15 00:00:00
PB - American Society for Microbiology
SP - 3151-3161
IS - 10
VL - 28
PMID - 18332120
SN - 0270-7306
SN - 1098-5549
ER -
Cite this
BibTex
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@article{2008_White,
author = {Joshua White and Richa Sardana and Janusz M. Bujnicki and Edward M. Marcotte and Arlen W Johnson and Zhihua Li},
title = {Bud23 Methylates G1575 of 18S rRNA and Is Required for Efficient Nuclear Export of Pre-40S Subunits},
journal = {Molecular and Cellular Biology},
year = {2008},
volume = {28},
publisher = {American Society for Microbiology},
month = {may},
url = {https://doi.org/10.1128%2FMCB.01674-07},
number = {10},
pages = {3151--3161},
doi = {10.1128/MCB.01674-07}
}
Cite this
MLA
Copy
White, Joshua, et al. “Bud23 Methylates G1575 of 18S rRNA and Is Required for Efficient Nuclear Export of Pre-40S Subunits.” Molecular and Cellular Biology, vol. 28, no. 10, May. 2008, pp. 3151-3161. https://doi.org/10.1128%2FMCB.01674-07.