Effect of point mutations in the decoding site (C1400) region of 16S ribosomal RNA on the ability of ribosomes to carry out individual steps of protein synthesis

Biochemistry ◽  
1989 ◽  
Vol 28 (3) ◽  
pp. 1012-1019 ◽  
Author(s):  
Robert Denman ◽  
Didier Negre ◽  
Philip R. Cunningham ◽  
Kelvin Nurse ◽  
John Colgan ◽  
...  
Biochemistry ◽  
2013 ◽  
Vol 52 (38) ◽  
pp. 6695-6701 ◽  
Author(s):  
Bhubanananda Sahu ◽  
Prashant K. Khade ◽  
Simpson Joseph

2021 ◽  
Author(s):  
Zhuo Bi ◽  
Hong-Wei Su ◽  
Jia-Yao Hong ◽  
Babak Javid

SummaryDespite redundant cellular pathways to minimize translational errors, errors in protein synthesis are common. Pathways and mechanisms to minimize errors are classified as pre-ribosomal or ribosomal. Pre-ribosomal pathways are primarily concerned with appropriate pairing of tRNAs with their cognate amino acid, whereas to date, ribosomal proof-reading has been thought to only be concerned with minimizing decoding errors, since it has been assumed that the ribosomal decoding centre is blind to mischarged tRNAs. Here, we identified that in mycobacteria, deletion of the 16S ribosomal RNA methyltransferase gidB led to increased discrimination of mischarged tRNAs. GidB deletion was necessary but not sufficient for reducing mistranslation due to misacylation. Discrimination only occurred in mycobacteria enriched from environments or genetic backgrounds with high rates of mistranslation. Our data suggest that mycobacterial ribosomes are capable of discriminating mischarged tRNAs and that 16S rRNA methylation by GidB may act as a capacitor for moderating translational error.


2019 ◽  
Vol 36 (12) ◽  
pp. 2854-2860 ◽  
Author(s):  
Iddo Weiner ◽  
Noam Shahar ◽  
Pini Marco ◽  
Iftach Yacoby ◽  
Tamir Tuller

Abstract Chloroplasts originated from an ancient cyanobacterium and still harbor a bacterial-like genome. However, the centrality of Shine–Dalgarno ribosome binding, which predominantly regulates proteobacterial translation initiation, is significantly decreased in chloroplasts. As plastid ribosomal RNA anti-Shine–Dalgarno elements are similar to their bacterial counterparts, these sites alone cannot explain this decline. By computational simulation we show that upstream point mutations modulate the local structure of ribosomal RNA in chloroplasts, creating significantly tighter structures around the anti-Shine–Dalgarno locus, which in-turn reduce the probability of ribosome binding. To validate our model, we expressed two reporter genes (mCherry, hydrogenase) harboring a Shine–Dalgarno motif in the Chlamydomonas reinhardtii chloroplast. Coexpressing them with a 16S ribosomal RNA, modified according to our model, significantly enhances mCherry and hydrogenase expression compared with coexpression with an endogenous 16S gene.


1991 ◽  
Vol 10 (8) ◽  
pp. 2203-2214 ◽  
Author(s):  
T. Powers ◽  
H.F. Noller

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