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Literature summary for 3.6.5.3 extracted from

  • Brandi, A.; Piersimoni, L.; Feto, N.A.; Spurio, R.; Alix, J.H.; Schmidt, F.; Gualerzi, C.O.
    Translation initiation factor IF2 contributes to ribosome assembly and maturation during cold adaptation (2019), Nucleic Acids Res., 47, 4652-4662 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene inB, recombinant expression in Escherichia coli strain BL21infB::kanR, that has an inactivated endogenous infB gene Escherichia coli

Protein Variants

Protein Variants Comment Organism
E571K the IF2alpha mutant has a completely inactivated GTPase activity Escherichia coli
additional information construction of a IF2alphaDELTA GTPase mutant with abolished GTPase activity Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
ribosome
-
Escherichia coli 5840
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GTP + H2O Escherichia coli
-
GDP + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A705
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP + H2O
-
Escherichia coli GDP + phosphate
-
?
additional information IF2 has protein chaperone activity. It catalyzes the refolding of heat-denatured GFP upon incubation for 8 min at 25°C at chaperone/GFP stoichiometric ratios of 1:1 carried out in buffer containing 1 mM GTP and 1 mM ATP. IF2alpha displays the highest chaperone activity in the presence of GTP, and its activity is substantially reduced, albeit not completely abolished, in the presence of GDP, or of the non-hydrolysable analogue GDPCP or in the absence of guanine nucleotides Escherichia coli ?
-
-

Synonyms

Synonyms Comment Organism
IF2
-
Escherichia coli
IF2alpha
-
Escherichia coli
infB
-
Escherichia coli
translation initiation factor
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
17
-
chaperone activity assay at Escherichia coli
25
-
GTPase assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Escherichia coli

Expression

Organism Comment Expression
Escherichia coli cold stress in Escherichia coli induces de novo synthesis of translation initiation factors IF1, IF2 and IF3 while ribosome synthesis and assembly slow down up

General Information

General Information Comment Organism
malfunction two cold-sensitive IF2 mutations cause the accumulation of immature ribosomal particles Escherichia coli
metabolism IF1 and IF3 increase plays a role in translation regulation at low temperature (cold-shock-induced translational bias) while the increase in IF2 made after cold stress is associated with immature ribosomal subunits together with at least another nine proteins involved in assembly and/or maturation of ribosomal subunits. IF2 is endowed with GTPase-associated chaperone activity that promotes refolding of denatured GFP Escherichia coli
physiological function translation initiation factor IF2 contributes to ribosome assembly and maturation during cold adaptation. IF2 is endowed with GTPase-associated chaperone activity that promotes refolding of denatured GFP. IF2 is another GTPase protein that participates in ribosome assembly/maturation, especially at low temperatures, the GTPase activity takes part in the assembly and maturation of the ribosomal subunits. The functional role of IF2 cannot be regarded as being restricted to its well documented functions in translation initiation of bacterial mRNA. IF2 has protein chaperone activity. For assembly and maturation of the ribosomal subunits, the cell requires an increased number of IF2 molecules, it is essential during the cold acclimation phase which follows cold stress when this process becomes particularly critical Escherichia coli