scholarly journals The enigma of the gene coding for ribosomal protein S12 in the chtoroplasts of Nicotiana

1986 ◽  
Vol 14 (2) ◽  
pp. 883-898 ◽  
Author(s):  
H. Fromm ◽  
M. Edelman ◽  
B. Koller ◽  
P. Goloubinoff ◽  
E. Galun
Keyword(s):  
Ribosomal Protein ◽  
Gene Coding ◽  
Ribosomal Protein S12

scholarly journals Cloning and sequencing of mouse ribosomal protein S12 cDNA

1989 ◽  
Vol 17 (16) ◽  
pp. 6722-6722 ◽  
Author(s):  
Mohamed Ayane ◽  
Peter Nielsen ◽  
Georges Köhler
Keyword(s):  
Ribosomal Protein ◽  
Cloning And Sequencing ◽  
Ribosomal Protein S12

An intergenic G-rich region in Leishmania tarentolae kinetoplast maxicircle DNA is a pan-edited cryptogene encoding ribosomal protein S12

1992 ◽  
Vol 12 (1) ◽  
pp. 56-67
Author(s):  
D A Maslov ◽  
N R Sturm ◽  
B M Niner ◽  
E S Gruszynski ◽  
M Peris ◽  
...  
Keyword(s):  
Amino Acid ◽  
Ribosomal Protein ◽  
Ribosomal Proteins ◽  
Sequence Similarity ◽  
Rich Region ◽  
Leishmania Tarentolae ◽  
Significant Sequence Similarity ◽  
The Family ◽  
Intergenic Regions ◽  
Ribosomal Protein S12

Six short G-rich intergenic regions in the maxicircle of Leishmania tarentolae are conserved in location and polarity in two other kinetoplastid species. We show here that G-rich region 6 (G6) represents a pan-edited cryptogene which contains at least two domains edited independently in a 3'-to-5' manner connected by short unedited regions. In the completely edited RNA, 117 uridines are added at 49 sites and 32 uridines are deleted at 13 sites, creating a translated 85-amino-acid polypeptide. Similar polypeptides are probably encoded by pan-edited G6 transcripts in two other species. The G6 polypeptide has significant sequence similarity to the family of S12 ribosomal proteins. A minicircle-encoded gRNA overlaps 12 editing sites in G6 mRNA, and chimeric gRNA/mRNA molecules were shown to exist, in agreement with the transesterification model for editing.

scholarly journals The 5' untranslated region of mRNA for ribosomal protein S19 is involved in its translational regulation during Xenopus development.

1990 ◽  
Vol 10 (2) ◽  
pp. 816-822 ◽  
Author(s):  
P Mariottini ◽  
F Amaldi
Keyword(s):  
Ribosomal Protein ◽  
Untranslated Region ◽  
Ribosomal Proteins ◽  
Translational Regulation ◽  
Xenopus Development ◽  
Untranslated Sequence ◽  
Gene Coding ◽  
Ribosomal Protein S19 ◽  
Fused Gene

During Xenopus development, the synthesis of ribosomal proteins is regulated at the translational level. To identify the region of the ribosomal protein mRNAs responsible for their typical translational behavior, we constructed a fused gene in which the upstream sequences (promoter) and the 5' untranslated sequence (first exon) of the gene coding for Xenopus ribosomal protein S19 were joined to the coding portion of the procaryotic chloramphenicol acetyltransferase (CAT) gene deleted of its own 5' untranslated region. This fused gene was introduced in vivo by microinjection into Xenopus fertilized eggs, and its activity was monitored during embryogenesis. By analyzing the pattern of appearance of CAT activity and the distribution of the S19-CAT mRNA between polysomes and messenger ribonucleoproteins, it was concluded that the 35-nucleotide-long 5' untranslated region of the S19 mRNA is able to confer to the fused S19-CAT mRNA the translational behavior typical of ribosomal proteins during Xenopus embryo development.

Simultaneous Horizontal Gene Transfer of a Gene Coding for Ribosomal Protein L27 and Operational Genes in Arthrobacter Sp.

2002 ◽  
Vol 55 (6) ◽  
pp. 632-637 ◽  
Author(s):  
Santiago Garcia-Vallvé ◽  
Francesc X. Simó ◽  
Miguel A. Montero ◽  
Lluís Arola ◽  
Antoni Romeu
Keyword(s):  
Gene Transfer ◽  
Horizontal Gene Transfer ◽  
Ribosomal Protein ◽  
Gene Coding

Modulation of 16S rRNA function by ribosomal protein S12

2007 ◽  
Vol 1769 (7-8) ◽  
pp. 462-471 ◽  
Author(s):  
Anton Vila-Sanjurjo ◽  
Ying Lu ◽  
Jamie L. Aragonez ◽  
Rebekah E. Starkweather ◽  
Manoj Sasikumar ◽  
...  
Keyword(s):  
16S Rrna ◽  
Ribosomal Protein ◽  
Ribosomal Protein S12

scholarly journals Resistance to the Peptidyl Transferase Inhibitor Tiamulin Caused by Mutation of Ribosomal Protein L3

2003 ◽  
Vol 47 (9) ◽  
pp. 2892-2896 ◽  
Author(s):  
Jacob Bøsling ◽  
Susan M. Poulsen ◽  
Birte Vester ◽  
Katherine S. Long
Keyword(s):  
Ribosomal Protein ◽  
Drug Binding ◽  
Mechanisms Of Resistance ◽  
Peptidyl Transferase ◽  
Peptidyl Transferase Center ◽  
Resistance Determinants ◽  
Drug Binding Site ◽  
Gene Coding ◽  
Bacterial Ribosome ◽  
Ribosomal Protein L3

ABSTRACT The antibiotic tiamulin targets the 50S subunit of the bacterial ribosome and interacts at the peptidyl transferase center. Tiamulin-resistant Escherichia coli mutants were isolated in order to elucidate mechanisms of resistance to the drug. No mutations in the rRNA were selected as resistance determinants using a strain expressing only a plasmid-encoded rRNA operon. Selection in a strain with all seven chromosomal rRNA operons yielded a mutant with an A445G mutation in the gene coding for ribosomal protein L3, resulting in an Asn149Asp alteration. Complementation experiments and sequencing of transductants demonstrate that the mutation is responsible for the resistance phenotype. Chemical footprinting experiments show a reduced binding of tiamulin to mutant ribosomes. It is inferred that the L3 mutation, which points into the peptidyl transferase cleft, causes tiamulin resistance by alteration of the drug-binding site. This is the first report of a mechanism of resistance to tiamulin unveiled in molecular detail.

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