scholarly journals Structural analysis of three prokaryotic 5S rRNA species and selected 5S rRNA-ribosomal-protein complexes by means of Pb(II)-induced hydrolysis

1992 ◽  
Vol 204 (2) ◽  
pp. 575-581 ◽  
Author(s):  
Jerzy CIESIOLKA ◽  
Siegfried LORENZ ◽  
Volker A. ERDMANN
Keyword(s):  
Structural Analysis ◽  
Ribosomal Protein ◽  
Protein Complexes ◽  
5S Rrna ◽  
Rrna Species

scholarly journals Nucleophosmin Is Essential for Ribosomal Protein L5 Nuclear Export

2006 ◽  
Vol 26 (10) ◽  
pp. 3798-3809 ◽  
Author(s):  
Yue Yu ◽  
Leonard B. Maggi ◽  
Suzanne N. Brady ◽  
Anthony J. Apicelli ◽  
Mu-Shui Dai ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Nuclear Export ◽  
Ribosome Biogenesis ◽  
Protein Complexes ◽  
Direct Interaction ◽  
5S Rrna ◽  
Centrosome Duplication ◽  
Ribosomal Subunits ◽  
Cycle Arrest ◽  
Ribosomal Protein L5

ABSTRACT Nucleophosmin (NPM/B23) is a key regulator in the regulation of a number of processes including centrosome duplication, maintenance of genomic integrity, and ribosome biogenesis. While the mechanisms underlying NPM function are largely uncharacterized, NPM loss results in severe dysregulation of developmental and growth-related events. We show that NPM utilizes a conserved CRM1-dependent nuclear export sequence in its amino terminus to enable its shuttling between the nucleolus/nucleus and cytoplasm. In search of NPM trafficking targets, we biochemically purified NPM-bound protein complexes from HeLa cell lysates. Consistent with NPM's proposed role in ribosome biogenesis, we isolated ribosomal protein L5 (rpL5), a known chaperone for the 5S rRNA. Direct interaction of NPM with rpL5 mediated the colocalization of NPM with maturing nuclear 60S ribosomal subunits, as well as newly exported and assembled 80S ribosomes and polysomes. Inhibition of NPM shuttling or loss of NPM blocked the nuclear export of rpL5 and 5S rRNA, resulting in cell cycle arrest and demonstrating that NPM and its nuclear export provide a unique and necessary chaperoning activity to rpL5/5S.

scholarly journals Structural analysis of 5S rRNA, 5S rRNA-protein complexes and ribosomes employing RNase H and d(GTTCGG)

1987 ◽  
Vol 163 (2) ◽  
pp. 239-246 ◽  
Author(s):  
Siegfried LORENZ ◽  
Roland K. HARTMANN ◽  
Norbert PIEL ◽  
Norbert ULBRICH ◽  
Volker A. ERDMANN
Keyword(s):  
Structural Analysis ◽  
Protein Complexes ◽  
Rnase H ◽  
5S Rrna

scholarly journals Structural analysis of two plant 5S rRNA species and fragments thereof by lead-induced hydrolysis

IUBMB Life ◽  
1996 ◽  
Vol 39 (2) ◽  
pp. 319-328
Author(s):  
Jerzy Ciesiołka ◽  
Włodzimierz Krzyzosiak
Keyword(s):  
Structural Analysis ◽  
5S Rrna ◽  
Rrna Species

scholarly journals Isolation and structural analysis of a ribosomal protein gene inD.melanogaster

1988 ◽  
Vol 16 (11) ◽  
pp. 4915-4926 ◽  
Author(s):  
F. Rafti ◽  
G. Gargiulo ◽  
A. Manzi ◽  
C. Malva ◽  
G. Grossi ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Ribosomal Protein ◽  
Protein Gene ◽  
Ribosomal Protein Gene

Mutational and Structural Analysis of the RNA Binding Site for Escherichia coli Ribosomal Protein S7

1994 ◽  
Vol 244 (1) ◽  
pp. 74-85 ◽  
Author(s):  
François Dragon ◽  
Catherine Payant ◽  
Léa Brakier-Gingras
Keyword(s):  
Escherichia Coli ◽  
Structural Analysis ◽  
Ribosomal Protein ◽  
Binding Site ◽  
Rna Binding

Yeast ribosomal protein L1 is required for the stability of newly synthesized 5S rRNA and the assembly of 60S ribosomal subunits

1993 ◽  
Vol 13 (5) ◽  
pp. 2835-2845
Author(s):  
M Deshmukh ◽  
Y F Tsay ◽  
A G Paulovich ◽  
J L Woolford
Keyword(s):  
Ribosomal Protein ◽  
Ribosomal Subunit ◽  
Single Copy ◽  
5S Rrna ◽  
Gene Encoding ◽  
Ribosomal Subunits ◽  
Ribosomal Protein L1 ◽  
The Stability ◽  
And Function

Ribosomal protein L1 from Saccharomyces cerevisiae binds 5S rRNA and can be released from intact 60S ribosomal subunits as an L1-5S ribonucleoprotein (RNP) particle. To understand the nature of the interaction between L1 and 5S rRNA and to assess the role of L1 in ribosome assembly and function, we cloned the RPL1 gene encoding L1. We have shown that RPL1 is an essential single-copy gene. A conditional null mutant in which the only copy of RPL1 is under control of the repressible GAL1 promoter was constructed. Depletion of L1 causes instability of newly synthesized 5S rRNA in vivo. Cells depleted of L1 no longer assemble 60S ribosomal subunits, indicating that L1 is required for assembly of stable 60S ribosomal subunits but not 40S ribosomal subunits. An L1-5S RNP particle not associated with ribosomal particles was detected by coimmunoprecipitation of L1 and 5S rRNA. This pool of L1-5S RNP remained stable even upon cessation of 60S ribosomal subunit assembly by depletion of another ribosomal protein, L16. Preliminary results suggest that transcription of RPL1 is not autogenously regulated by L1.

Mutual Induced Fit Binding of Xenopus Ribosomal Protein L5 to 5S rRNA

2003 ◽  
Vol 330 (5) ◽  
pp. 979-992 ◽  
Author(s):  
Jonathan P. DiNitto ◽  
Paul W. Huber
Keyword(s):  
Ribosomal Protein ◽  
5S Rrna ◽  
Induced Fit ◽  
Ribosomal Protein L5

Developmental expression and 5S rRNA-binding activity of Xenopus laevis ribosomal protein L5

1989 ◽  
Vol 9 (12) ◽  
pp. 5281-5288
Author(s):  
W M Wormington
Keyword(s):  
Ribosomal Protein ◽  
Mammalian Cells ◽  
Ribosomal Proteins ◽  
5S Rrna ◽  
Yeast Cells ◽  
Developmental Expression ◽  
Rrna Synthesis ◽  
Ribosome Assembly ◽  
Subunit Assembly ◽  
Ribosomal Protein L5

Ribosomal protein L5 binds specifically to 5S rRNA to form a complex that is a precursor to 60S subunit assembly in vivo. Analyses in yeast cells, mammalian cells, and Xenopus embryos have shown that the accumulation of L5 is not coordinated with the expression of other ribosomal proteins. In this study, the primary structure and developmental expression of Xenopus ribosomal protein L5 were examined to determine the basis for its distinct regulation. These analyses showed that L5 expression could either coincide with 5S rRNA synthesis and ribosome assembly or be controlled independently of these events at different stages of Xenopus development. L5 synthesis during oogenesis was uncoupled from the accumulation of 5S rRNa but coincided with subunit assembly. In early embryos, the inefficient translation of L5 mRNA resulted in the accumulation of a stable L5-5S rRNA complex before ribosome assembly at later stages of development. Additional results demonstrated that L5 protein synthesized in vitro bound specifically to 5S rRNA.

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