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 Role and dynamics of the ribosomal protein P0 and its related trans -acting factor Mrt4 during ribosome assembly in Saccharomyces cerevisiae

2009 ◽  
Vol 37 (22) ◽  
pp. 7519-7532 ◽  
Author(s):  
María Rodríguez-Mateos ◽  
Juan J. García-Gómez ◽  
Rosario Francisco-Velilla ◽  
Miguel Remacha ◽  
Jesús de la Cruz ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Ribosomal Protein ◽  
Ribosome Assembly ◽  
Ribosomal Protein P0

scholarly journals Ribosomal protein L32 of Saccharomyces cerevisiae influences both the splicing of its own transcript and the processing of rRNA.

1997 ◽  
Vol 17 (4) ◽  
pp. 1959-1965 ◽  
Author(s):  
J Vilardell ◽  
J R Warner
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Ribosomal Protein ◽  
Ribosomal Subunit ◽  
Mutant Gene ◽  
Mutant Form ◽  
Hydrophobic Domain ◽  
Rna Molecules ◽  
Reduced Rate ◽  
And Function ◽  
Isoleucine Residue

Ribosomal protein L32 of Saccharomyces cerevisiae binds to and regulates the splicing and the translation of the transcript of its own gene. Selecting for mutants deficient in the regulation of splicing, we have identified a mutant form of L32 that no longer binds to the transcript of RPL32 and therefore does not regulate its splicing. The mutation is the deletion of an isoleucine residue from a highly conserved hydrophobic domain near the middle of L32. The mutant protein supports growth, at a reduced rate, and is found at normal levels in mature ribosomes. However, in cells homozygous for the mutant gene, the rate of processing of the ribosomal RNA component of the 60S ribosomal subunit is severely reduced, leading to an insufficiency of 60S subunits. L32 must be considered a remarkable protein. Composed of only 104 amino acids, it appears to interact with three distinct RNA molecules to influence three different elements of RNA processing and function in three different locations of the cell: the processing of pre-rRNA in the nucleolus, the splicing of the RPL32 transcript in the nucleus, and the translation of the spliced RPL32 mRNA in the cytoplasm.

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 DRS1 to DRS7, novel genes required for ribosome assembly and function in Saccharomyces cerevisiae.

1993 ◽  
Vol 13 (12) ◽  
pp. 7901-7912 ◽  
Author(s):  
T L Ripmaster ◽  
G P Vaughn ◽  
J L Woolford
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Elongation Factor ◽  
Ribosome Assembly ◽  
Predicted Amino Acid Sequence ◽  
Phosphate Binding ◽  
Ribosomal Subunits ◽  
Cold Sensitive ◽  
And Function

To identify Saccharomyces cerevisiae mutants defective in assembly or function of ribosomes, a collection of cold-sensitive strains generated by treatment with ethyl methanesulfonate was screened by sucrose gradient analysis for altered ratios of free 40S to 60S ribosomal subunits or qualitative changes in polyribosome profiles. Mutations defining seven complementation groups deficient in ribosomal subunits, drs1 to drs7, were identified. We have previously shown that DRS1 encodes a putative ATP-dependent RNA helicase necessary for assembly of 60S ribosomal subunits (T. L. Ripmaster, G. P. Vaughn, and J. L. Woolford, Jr., Proc. Natl. Acad. Sci. USA 89:11131-11135, 1992). Strains bearing the drs2 mutation process the 20S precursor of the mature 18S rRNA slowly and are deficient in 40S ribosomal subunits. Cloning and sequencing of the DRS2 gene revealed that it encodes a protein similar to membrane-spanning Ca2+ ATPases. The predicted amino acid sequence encoded by DRS2 contains seven transmembrane domains, a phosphate-binding loop found in ATP- or GTP-binding proteins, and a seven-amino-acid sequence detected in all classes of P-type ATPases. The cold-sensitive phenotype of drs2 is suppressed by extra copies of the TEF3 gene, which encodes a yeast homolog of eukaryotic translation elongation factor EF-1 gamma. Identification of gene products affecting ribosome assembly and function among the DNAs complementing the drs mutations validates the feasibility of this approach.

scholarly journals Role of the 40S beak ribosomal protein eS12 in ribosome biogenesis and function in Saccharomyces cerevisiae

RNA Biology ◽  
2020 ◽  
Vol 17 (9) ◽  
pp. 1261-1276
Author(s):  
Sara Martín-Villanueva ◽  
José Fernández-Fernández ◽  
Olga Rodríguez-Galán ◽  
Julia Fernández-Boraita ◽  
Eduardo Villalobo ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Ribosomal Protein ◽  
Ribosome Biogenesis ◽  
And Function

DRS1 to DRS7, novel genes required for ribosome assembly and function in Saccharomyces cerevisiae

1993 ◽  
Vol 13 (12) ◽  
pp. 7901-7912
Author(s):  
T L Ripmaster ◽  
G P Vaughn ◽  
J L Woolford
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Elongation Factor ◽  
Ribosome Assembly ◽  
Predicted Amino Acid Sequence ◽  
Phosphate Binding ◽  
Ribosomal Subunits ◽  
Cold Sensitive ◽  
And Function

To identify Saccharomyces cerevisiae mutants defective in assembly or function of ribosomes, a collection of cold-sensitive strains generated by treatment with ethyl methanesulfonate was screened by sucrose gradient analysis for altered ratios of free 40S to 60S ribosomal subunits or qualitative changes in polyribosome profiles. Mutations defining seven complementation groups deficient in ribosomal subunits, drs1 to drs7, were identified. We have previously shown that DRS1 encodes a putative ATP-dependent RNA helicase necessary for assembly of 60S ribosomal subunits (T. L. Ripmaster, G. P. Vaughn, and J. L. Woolford, Jr., Proc. Natl. Acad. Sci. USA 89:11131-11135, 1992). Strains bearing the drs2 mutation process the 20S precursor of the mature 18S rRNA slowly and are deficient in 40S ribosomal subunits. Cloning and sequencing of the DRS2 gene revealed that it encodes a protein similar to membrane-spanning Ca2+ ATPases. The predicted amino acid sequence encoded by DRS2 contains seven transmembrane domains, a phosphate-binding loop found in ATP- or GTP-binding proteins, and a seven-amino-acid sequence detected in all classes of P-type ATPases. The cold-sensitive phenotype of drs2 is suppressed by extra copies of the TEF3 gene, which encodes a yeast homolog of eukaryotic translation elongation factor EF-1 gamma. Identification of gene products affecting ribosome assembly and function among the DNAs complementing the drs mutations validates the feasibility of this approach.

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