» Articles » PMID: 17517959

Intranucleolar Sites of Ribosome Biogenesis Defined by the Localization of Early Binding Ribosomal Proteins

Overview
Journal J Cell Biol
Specialty Cell Biology
Date 2007 May 23
PMID 17517959
Citations 24
Authors
Affiliations
Soon will be listed here.
Abstract

Considerable efforts are being undertaken to elucidate the processes of ribosome biogenesis. Although various preribosomal RNP complexes have been isolated and molecularly characterized, the order of ribosomal protein (r-protein) addition to the emerging ribosome subunits is largely unknown. Furthermore, the correlation between the ribosome assembly pathway and the structural organization of the dedicated ribosome factory, the nucleolus, is not well established. We have analyzed the nucleolar localization of several early binding r-proteins in human cells, applying various methods, including live-cell imaging and electron microscopy. We have located all examined r-proteins (S4, S6, S7, S9, S14, and L4) in the granular component (GC), which is the nucleolar region where later pre-ribosomal RNA (rRNA) processing steps take place. These results imply that early binding r-proteins do not assemble with nascent pre-rRNA transcripts in the dense fibrillar component (DFC), as is generally believed, and provide a link between r-protein assembly and the emergence of distinct granules at the DFC-GC interface.

Citing Articles

Ribosomal protein L24 mediates mammalian microRNA processing in an evolutionarily conserved manner.

Tzur Y, Dubnov S, Madrer N, Bar A, Nadorp B, Mishra N Cell Mol Life Sci. 2024; 81(1):55.

PMID: 38261097 PMC: 10805976. DOI: 10.1007/s00018-023-05088-w.


Nucleolar dynamics are determined by the ordered assembly of the ribosome.

Sheu-Gruttadauria J, Yan X, Stuurman N, Vale R, Floor S bioRxiv. 2023; .

PMID: 37808656 PMC: 10557630. DOI: 10.1101/2023.09.26.559432.


Viscoelasticity and advective flow of RNA underlies nucleolar form and function.

Riback J, Eeftens J, Lee D, Quinodoz S, Donlic A, Orlovsky N Mol Cell. 2023; 83(17):3095-3107.e9.

PMID: 37683610 PMC: 11089468. DOI: 10.1016/j.molcel.2023.08.006.


The exon-junction complex helicase eIF4A3 controls cell fate via coordinated regulation of ribosome biogenesis and translational output.

Kanellis D, Espinoza J, Zisi A, Sakkas E, Bartkova J, Katsori A Sci Adv. 2021; 7(32).

PMID: 34348895 PMC: 8336962. DOI: 10.1126/sciadv.abf7561.


High resolution RNA-seq profiling of genes encoding ribosomal proteins across different organs and developmental stages in .

Xiong W, Zhang J, Lan T, Kong W, Wang X, Liu L Plant Direct. 2021; 5(5):e00320.

PMID: 34095740 PMC: 8156134. DOI: 10.1002/pld3.320.


References
1.
Elkon K, Skelly S, Parnassa A, Moller W, Danho W, Weissbach H . Identification and chemical synthesis of a ribosomal protein antigenic determinant in systemic lupus erythematosus. Proc Natl Acad Sci U S A. 1986; 83(19):7419-23. PMC: 386729. DOI: 10.1073/pnas.83.19.7419. View

2.
El Hage A, Tollervey D . A surfeit of factors: why is ribosome assembly so much more complicated in eukaryotes than bacteria?. RNA Biol. 2006; 1(1):10-5. View

3.
Reimer G, Pollard K, Penning C, Ochs R, Lischwe M, Busch H . Monoclonal autoantibody from a (New Zealand black x New Zealand white)F1 mouse and some human scleroderma sera target an Mr 34,000 nucleolar protein of the U3 RNP particle. Arthritis Rheum. 1987; 30(7):793-800. DOI: 10.1002/art.1780300709. View

4.
Bachellerie J, PUVION E . Nucleolar organization of HeLa cells as studied by in situ hybridization. Chromosoma. 1991; 100(6):395-409. DOI: 10.1007/BF00337518. View

5.
Matera A, Tycowski K, Steitz J, Ward D . Organization of small nucleolar ribonucleoproteins (snoRNPs) by fluorescence in situ hybridization and immunocytochemistry. Mol Biol Cell. 1994; 5(12):1289-99. PMC: 301158. DOI: 10.1091/mbc.5.12.1289. View