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The Ribosomal Protein Rpl22 Controls Ribosome Composition by Directly Repressing Expression of Its Own Paralog,Rpl22l1
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نویسنده
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o'leary m.n. ,schreiber k.h. ,zhang y. ,duc a.-c.e. ,rao s. ,hale j.s. ,academia e.c. ,shah s.r. ,morton j.f. ,holstein c.a. ,martin d.b. ,kaeberlein m. ,ladiges w.c. ,fink p.j. ,mackay v.l. ,wiest d.l. ,kennedy b.k.
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منبع
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plos genetics - 2013 - دوره : 9 - شماره : 8
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چکیده
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Most yeast ribosomal protein genes are duplicated and their characterization has led to hypotheses regarding the existence of specialized ribosomes with different subunit composition or specifically-tailored functions. in yeast,ribosomal protein genes are generally duplicated and evidence has emerged that paralogs might have specific roles. unlike yeast,most mammalian ribosomal proteins are thought to be encoded by a single gene copy,raising the possibility that heterogenous populations of ribosomes are unique to yeast. here,we examine the roles of the mammalian rpl22,finding that rpl22-/- mice have only subtle phenotypes with no significant translation defects. we find that in the rpl22-/- mouse there is a compensatory increase in rpl22-like1 (rpl22l1) expression and incorporation into ribosomes. consistent with the hypothesis that either ribosomal protein can support translation,knockdown of rpl22l1 impairs growth of cells lacking rpl22. mechanistically,rpl22 regulates rpl22l1 directly by binding to an internal hairpin structure and repressing its expression. we propose that ribosome specificity may exist in mammals,providing evidence that one ribosomal protein can influence composition of the ribosome by regulating its own paralog. © 2013 o'leary et al.
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آدرس
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department of biochemistry,university of washington,seattle,wa,united states,buck institute for research on aging,novato,ca, United States, department of biochemistry,university of washington,seattle,wa,united states,buck institute for research on aging,novato,ca, United States, blood cell development and cancer keystone,immune cell development and host defense program,fox chase cancer center,philadelphia,pa, United States, blood cell development and cancer keystone,immune cell development and host defense program,fox chase cancer center,philadelphia,pa, United States, blood cell development and cancer keystone,immune cell development and host defense program,fox chase cancer center,philadelphia,pa, United States, department of immunology,university of washington,seattle,wa,united states,emory university,atlanta,ga, United States, buck institute for research on aging,novato,ca, United States, department of biochemistry,university of washington,seattle,wa, United States, department of comparative medicine,university of washington,seattle,wa, United States, institute for systems biology,seattle,wa, United States, institute for systems biology,seattle,wa, United States, department of pathology,university of washington,seattle,wa, United States, department of comparative medicine,university of washington,seattle,wa, United States, department of immunology,university of washington,seattle,wa, United States, department of biochemistry,university of washington,seattle,wa, United States, blood cell development and cancer keystone,immune cell development and host defense program,fox chase cancer center,philadelphia,pa, United States, department of biochemistry,university of washington,seattle,wa,united states,buck institute for research on aging,novato,ca, United States
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Authors
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