Nucleic Acids Research Advance Access originally published online on June 21, 2007
Nucleic Acids Research 2007 35(13):4503-4514; doi:10.1093/nar/gkm428
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Nucleic Acids Research, 2007, Vol. 35, No. 13 4503-4514
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Molecular Biology |
Functional conservation between structurally diverse ribosomal proteins from Drosophila melanogaster and Saccharomyces cerevisiae: fly L23a can substitute for yeast L25 in ribosome assembly and function
Department of Biological Sciences, Lehigh University, Bethlehem, PA 18015, USA
*To whom correspondence should be addressed. Tel: +610-758-3690; Fax: 610-758-4004; Email: vcw0{at}lehigh.edu
Received January 14, 2007. Revised May 11, 2007. Accepted May 11, 2007.
The proposed Drosophila melanogaster L23a ribosomal protein features a conserved C-terminal amino acid signature characteristic of other L23a family members and a unique N-terminal extension [Koyama et al. (Poly(ADP-ribose) polymerase interacts with novel Drosophila ribosomal proteins, L22 and l23a, with unique histone-like amino-terminal extensions. Gene 1999; 226: 339–345)], absent from Saccharomyces cerevisiae L25 that nearly doubles the size of fly L23a. The ability of fly L23a to replace the role of yeast L25 in ribosome biogenesis was determined by creating a yeast strain carrying an L25 chromosomal gene disruption and a plasmid-encoded FLAG-tagged L23a gene. Though affected by a reduced growth rate, the strain is dependent on fly L23a-FLAG function for survival and growth, demonstrating functional compatibility between the fly and yeast proteins. Pulse-chase experiments reveal a delay in rRNA processing kinetics, most notably at a late cleavage step that converts precursor 27S rRNA into mature 25S rRNA, likely contributing to the strain's slower growth pattern. Yet, given the essential requirement for L23(a)/L25 in ribosome biogenesis, there is a remarkable tolerance for accommodating the fly L23a N-terminal extension within the structure of the yeast ribosome. A search of available databases shows that the unique N-terminal extension is shared by multiple insect lineages. An evolutionary perspective on L23a structure and function within insect lineages is discussed.
Present addresses: Ranoo R. Patel, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261, USA Tamra C. Mendelson, Department of Biological Sciences, University of Maryland, Baltimore County, Baltimore, MD 21250, USA
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