De novo Synthesis and Assembly of rRNA into Ribosomal Subunits during Cold Acclimation in Escherichia coli

2016 ◽  
Vol 428 (8) ◽  
pp. 1558-1573 ◽  
Author(s):  
Lolita Piersimoni ◽  
Mara Giangrossi ◽  
Paolo Marchi ◽  
Anna Brandi ◽  
Claudio O. Gualerzi ◽  
...  
PLoS ONE ◽  
2014 ◽  
Vol 9 (7) ◽  
pp. e101492 ◽  
Author(s):  
Junjun Wu ◽  
Tiantian Zhou ◽  
Guocheng Du ◽  
Jingwen Zhou ◽  
Jian Chen

1978 ◽  
Vol 190 (2) ◽  
pp. 385-397 ◽  
Author(s):  
Kichitaro Kawaguchi ◽  
Jeffrey Fox ◽  
Eric Holmes ◽  
Charles Boyer ◽  
Jack Preiss

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Bo Eng Cheong ◽  
Olga Beine-Golovchuk ◽  
Michal Gorka ◽  
William Wing Ho Ho ◽  
Federico Martinez-Seidel ◽  
...  

AbstractArabidopsis REIL proteins are cytosolic ribosomal 60S-biogenesis factors. After shift to 10 °C, reil mutants deplete and slowly replenish non-translating eukaryotic ribosome complexes of root tissue, while controlling the balance of non-translating 40S- and 60S-subunits. Reil mutations respond by hyper-accumulation of non-translating subunits at steady-state temperature; after cold-shift, a KCl-sensitive 80S sub-fraction remains depleted. We infer that Arabidopsis may buffer fluctuating translation by pre-existing non-translating ribosomes before de novo synthesis meets temperature-induced demands. Reil1 reil2 double mutants accumulate 43S-preinitiation and pre-60S-maturation complexes and alter paralog composition of ribosomal proteins in non-translating complexes. With few exceptions, e.g. RPL3B and RPL24C, these changes are not under transcriptional control. Our study suggests requirement of de novo synthesis of eukaryotic ribosomes for long-term cold acclimation, feedback control of NUC2 and eIF3C2 transcription and links new proteins, AT1G03250, AT5G60530, to plant ribosome biogenesis. We propose that Arabidopsis requires biosynthesis of specialized ribosomes for cold acclimation.


2006 ◽  
Vol 188 (5) ◽  
pp. 1786-1797 ◽  
Author(s):  
Ekaterina N. Andreishcheva ◽  
Willie F. Vann

ABSTRACT Escherichia coli K1 is responsible for 80% of E. coli neonatal meningitis and is a common pathogen in urinary tract infections. Bacteria of this serotype are encapsulated with the α(2-8)-polysialic acid NeuNAc(α2-8), common to several bacterial pathogens. The gene cluster encoding the pathway for synthesis of this polymer is organized into three regions: (i) kpsSCUDEF, (ii) neuDBACES, and (iii) kpsMT. The K1 polysialyltransferase, NeuS, cannot synthesize polysialic acid de novo without other products of the gene cluster. Membranes isolated from strains having the entire K1 gene cluster can synthesize polysialic acid de novo. We designed a series of plasmid constructs containing fragments of regions 1 and 2 in two compatible vectors to determine the minimum number of gene products required for de novo synthesis of the polysialic acid from CMP-NeuNAc in K1 E. coli. We measured the ability of the various combinations of region 1 and 2 fragments to restore polysialyltransferase activity in vitro in the absence of exogenously added polysaccharide acceptor. The products of region 2 genes neuDBACES alone were not sufficient to support de novo synthesis of polysialic acid in vitro. Only membrane fractions harboring NeuES and KpsCS could form sialic polymer in the absence of exogenous acceptor at the concentrations formed by wild-type E. coli K1 membranes. Membrane fractions harboring NeuES and KpsC together could form small quantities of the sialic polymer de novo.


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