Title |
The 23 S rRNA environment of ribosomal protein L9 in the 50 S ribosomal subunit11Edited by D. E. Draper
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Published in |
Journal of Molecular Biology, April 2000
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DOI | 10.1006/jmbi.2000.3621 |
Pubmed ID | |
Authors |
Kate R Lieberman, Matthew A Firpo, Alan J Herr, Thuylinh Nguyenle, John F Atkins, Raymond F Gesteland, Harry F Noller |
Abstract |
Ribosomal protein L9 consists of two globular alpha/beta domains separated by a nine-turn alpha-helix. We examined the rRNA environment of L9 by chemical footprinting and directed hydroxyl radical probing. We reconstituted L9, or individual domains of L9, with L9-deficient 50 S subunits, or with deproteinized 23 S rRNA. A footprint was identified in domain V of 23 S rRNA that was mainly attributable to N-domain binding. Fe(II) was tethered to L9 via cysteine residues introduced at positions along the alpha-helix and in the C-domain, and derivatized proteins were reconstituted with L9-deficient subunits. Directed hydroxyl radical probing targeted regions of domains I, III, IV, and V of 23 S rRNA, reinforcing the view that 50 S subunit architecture is typified by interwoven rRNA domains. There was a striking correlation between the cleavage patterns from the Fe(II) probes attached to the alpha-helix and their predicted orientations, constraining both the position and orientation of L9, as well as the arrangement of specific elements of 23 S rRNA, in the 50 S subunit. |
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Geographical breakdown
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United States | 2 | 8% |
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Unknown | 20 | 83% |
Demographic breakdown
Readers by professional status | Count | As % |
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Student > Ph. D. Student | 5 | 21% |
Professor | 4 | 17% |
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Student > Master | 2 | 8% |
Other | 2 | 8% |
Unknown | 2 | 8% |
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Computer Science | 1 | 4% |
Other | 0 | 0% |
Unknown | 2 | 8% |