scholarly journals Mapping the essential structures of human ribosomal protein L7 for nuclear entry, ribosome assembly and function

FEBS Letters ◽  
2006 ◽  
Vol 580 (16) ◽  
pp. 3804-3810 ◽  
Author(s):  
J.-R. Ko ◽  
Jing-Ying Wu ◽  
R. Kirby ◽  
I-Fang Li ◽  
Alan Lin
Keyword(s):  
Ribosomal Protein ◽  
Ribosome Assembly ◽  
Nuclear Entry ◽  
Human Ribosomal Protein ◽  
And Function

scholarly journals Saccharomyces cerevisiae Ribosomal Protein L26 Is Not Essential for Ribosome Assembly and Function

2012 ◽  
Vol 32 (16) ◽  
pp. 3228-3241 ◽  
Author(s):  
R. Babiano ◽  
M. Gamalinda ◽  
J. L. Woolford ◽  
J. de la Cruz
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Ribosomal Protein ◽  
Ribosome Assembly ◽  
And Function

scholarly journals Ubiquitin and Ubiquitin-Like Proteins and Domains in Ribosome Production and Function: Chance or Necessity?

2021 ◽  
Vol 22 (9) ◽  
pp. 4359
Author(s):  
Sara Martín-Villanueva ◽  
Gabriel Gutiérrez ◽  
Dieter Kressler ◽  
Jesús de la Cruz
Keyword(s):  
Ribosomal Proteins ◽  
Ribosome Biogenesis ◽  
Ribosome Assembly ◽  
Cellular Processes ◽  
Substrate Protein ◽  
Precursor Proteins ◽  
Assembly Factors ◽  
Ubiquitin Moiety ◽  
And Function

Ubiquitin is a small protein that is highly conserved throughout eukaryotes. It operates as a reversible post-translational modifier through a process known as ubiquitination, which involves the addition of one or several ubiquitin moieties to a substrate protein. These modifications mark proteins for proteasome-dependent degradation or alter their localization or activity in a variety of cellular processes. In most eukaryotes, ubiquitin is generated by the proteolytic cleavage of precursor proteins in which it is fused either to itself, constituting a polyubiquitin precursor, or as a single N-terminal moiety to ribosomal proteins, which are practically invariably eL40 and eS31. Herein, we summarize the contribution of the ubiquitin moiety within precursors of ribosomal proteins to ribosome biogenesis and function and discuss the biological relevance of having maintained the explicit fusion to eL40 and eS31 during evolution. There are other ubiquitin-like proteins, which also work as post-translational modifiers, among them the small ubiquitin-like modifier (SUMO). Both ubiquitin and SUMO are able to modify ribosome assembly factors and ribosomal proteins to regulate ribosome biogenesis and function. Strikingly, ubiquitin-like domains are also found within two ribosome assembly factors; hence, the functional role of these proteins will also be highlighted.

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.

Human ribosomal protein S16 inhibits excision of the first intron from its own pre-mRNA

2010 ◽  
Vol 44 (1) ◽  
pp. 82-88 ◽  
Author(s):  
A. V. Ivanov ◽  
N. M. Parakhnevitch ◽  
A. A. Malygin ◽  
G. G. Karpova
Keyword(s):  
Ribosomal Protein ◽  
First Intron ◽  
Human Ribosomal Protein ◽  
Human Ribosomal Protein S16

Human ribosomal protein S13 inhibits splicing of its own pre-mRNA

2007 ◽  
Vol 41 (1) ◽  
pp. 44-51 ◽  
Author(s):  
N. M. Parakhnevitch ◽  
A. V. Ivanov ◽  
A. A. Malygin ◽  
G. G. Karpova
Keyword(s):  
Ribosomal Protein ◽  
Human Ribosomal Protein ◽  
Ribosomal Protein S13 ◽  
Human Ribosomal Protein S13
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