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Ribosomal proteins L7 and L8 function in concert with six A₃ assembly factors to propagate assembly of domains I and II of 25S rRNA in yeast 60S ribosomal subunits.
RNA. 2012 Oct; 18(10):1805-22.RNA

Abstract

Ribosome biogenesis is a complex multistep process that involves alternating steps of folding and processing of pre-rRNAs in concert with assembly of ribosomal proteins. Recently, there has been increased interest in the roles of ribosomal proteins in eukaryotic ribosome biogenesis in vivo, focusing primarily on their function in pre-rRNA processing. However, much less is known about participation of ribosomal proteins in the formation and rearrangement of preribosomal particles as they mature to functional subunits. We have studied ribosomal proteins L7 and L8, which are required for the same early steps in pre-rRNA processing during assembly of 60S subunits but are located in different domains within ribosomes. Depletion of either leads to defects in processing of 27SA(3) to 27SB pre-rRNA and turnover of pre-rRNAs destined for large ribosomal subunits. A specific subset of proteins is diminished from these residual assembly intermediates: six assembly factors required for processing of 27SA(3) pre-rRNA and four ribosomal proteins bound to domain I of 25S and 5.8S rRNAs surrounding the polypeptide exit tunnel. In addition, specific sets of ribosomal proteins are affected in each mutant: In the absence of L7, proteins bound to domain II, L6, L14, L20, and L33 are greatly diminished, while proteins L13, L15, and L36 that bind to domain I are affected in the absence of L8. Thus, L7 and L8 might establish RNP structures within assembling ribosomes necessary for the stable association and function of the A(3) assembly factors and for proper assembly of the neighborhoods containing domains I and II.

Authors+Show Affiliations

Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

Language

eng

PubMed ID

22893726

Citation

Jakovljevic, Jelena, et al. "Ribosomal Proteins L7 and L8 Function in Concert With Six A₃ Assembly Factors to Propagate Assembly of Domains I and II of 25S rRNA in Yeast 60S Ribosomal Subunits." RNA (New York, N.Y.), vol. 18, no. 10, 2012, pp. 1805-22.
Jakovljevic J, Ohmayer U, Gamalinda M, et al. Ribosomal proteins L7 and L8 function in concert with six A₃ assembly factors to propagate assembly of domains I and II of 25S rRNA in yeast 60S ribosomal subunits. RNA. 2012;18(10):1805-22.
Jakovljevic, J., Ohmayer, U., Gamalinda, M., Talkish, J., Alexander, L., Linnemann, J., Milkereit, P., & Woolford, J. L. (2012). Ribosomal proteins L7 and L8 function in concert with six A₃ assembly factors to propagate assembly of domains I and II of 25S rRNA in yeast 60S ribosomal subunits. RNA (New York, N.Y.), 18(10), 1805-22. https://doi.org/10.1261/rna.032540.112
Jakovljevic J, et al. Ribosomal Proteins L7 and L8 Function in Concert With Six A₃ Assembly Factors to Propagate Assembly of Domains I and II of 25S rRNA in Yeast 60S Ribosomal Subunits. RNA. 2012;18(10):1805-22. PubMed PMID: 22893726.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Ribosomal proteins L7 and L8 function in concert with six A₃ assembly factors to propagate assembly of domains I and II of 25S rRNA in yeast 60S ribosomal subunits. AU - Jakovljevic,Jelena, AU - Ohmayer,Uli, AU - Gamalinda,Michael, AU - Talkish,Jason, AU - Alexander,Lisa, AU - Linnemann,Jan, AU - Milkereit,Philipp, AU - Woolford,John L,Jr Y1 - 2012/08/14/ PY - 2012/8/16/entrez PY - 2012/8/16/pubmed PY - 2012/12/10/medline SP - 1805 EP - 22 JF - RNA (New York, N.Y.) JO - RNA VL - 18 IS - 10 N2 - Ribosome biogenesis is a complex multistep process that involves alternating steps of folding and processing of pre-rRNAs in concert with assembly of ribosomal proteins. Recently, there has been increased interest in the roles of ribosomal proteins in eukaryotic ribosome biogenesis in vivo, focusing primarily on their function in pre-rRNA processing. However, much less is known about participation of ribosomal proteins in the formation and rearrangement of preribosomal particles as they mature to functional subunits. We have studied ribosomal proteins L7 and L8, which are required for the same early steps in pre-rRNA processing during assembly of 60S subunits but are located in different domains within ribosomes. Depletion of either leads to defects in processing of 27SA(3) to 27SB pre-rRNA and turnover of pre-rRNAs destined for large ribosomal subunits. A specific subset of proteins is diminished from these residual assembly intermediates: six assembly factors required for processing of 27SA(3) pre-rRNA and four ribosomal proteins bound to domain I of 25S and 5.8S rRNAs surrounding the polypeptide exit tunnel. In addition, specific sets of ribosomal proteins are affected in each mutant: In the absence of L7, proteins bound to domain II, L6, L14, L20, and L33 are greatly diminished, while proteins L13, L15, and L36 that bind to domain I are affected in the absence of L8. Thus, L7 and L8 might establish RNP structures within assembling ribosomes necessary for the stable association and function of the A(3) assembly factors and for proper assembly of the neighborhoods containing domains I and II. SN - 1469-9001 UR - https://www.unboundmedicine.com/medline/citation/22893726/Ribosomal_proteins_L7_and_L8_function_in_concert_with_six_A₃_assembly_factors_to_propagate_assembly_of_domains_I_and_II_of_25S_rRNA_in_yeast_60S_ribosomal_subunits_ L2 - http://www.rnajournal.org/cgi/pmidlookup?view=long&pmid=22893726 DB - PRIME DP - Unbound Medicine ER -