GenePage for the tufA gene of Escherichia coli K-12

Primary Gene Name: tufA
EcoGene Accession Number: EG11036
K-12 Gene Accession Number: ECK3326
MG1655 Gene Identifier: b3339
Gene Name Mnemonic: Translation unstable factor
Alternate Gene Symbols: kirT; pulT
Description: Translation elongation factor EF-Tu 1; GTP-dependent binding of aa-tRNA to the A-site of ribosomes; has intrinsic GTPase activity when bound to kirromycin
  # bp Upstream # bp Downstream
Verified Start MW: 43283.55 ---------394 aa Pre-Run BlastP UniProt
Pre-Run BlastP NR+Env
Left End: 3470145
Left Intergenic Region

Name: chiA_tufA

Length: 291 bp gap

Orientation: Codirectional-

Left_end: 3469854

Right_end: 3470144

Centisome: 74.75

Genomic Address
Counterclockwise
Minute or Centisome (%) = 74.76
Right End: 3471329
Right Intergenic Region

Name: tufA_fusA

Length: 70 bp gap

Orientation: Codirectional-

Left_end: 3471330

Right_end: 3471399

Centisome: 74.79

EF-Tu is the most abundant protein in E. coli comprising 5-10% of total cellular protein, well in excess of translational requirements (Furano, 1975; Jacobson, 1976; Neidhardt, 1977; Miyajima, 1978; Pedersen, 1978; Young, 1981; van der Meide, 1983). The only amino acid difference between TufA and TufB is the last amino acid, G394 in TufA and S394 in TufB. EF-Tu lysines K38, K177, K249, K253, K295 and K314 can be modified to N6-succinyllysine (Zhang, 2011). EF-Tu lysines K177, K188, K209 and K314 can be modified to N6-acetyllysine (Yu, 2008; Zhang, 2009). HipA binds and was reported to phosphorylate EF-Tu residue Thr-383 in vitro (Schumacher, 2009). HipA is not EF-Tu kinase (Germain, 2013). The phage P1 toxin Doc phosphorylates EF-Tu in vitro at Thr383, blocking its ability to bind aminoacylated tRNAs (Castro-Roa, 2013). EF-Tu can be modified at K57 to either N6-monomethyllysine or N6,N6-dimethyllysine; the methyltransferases responsible for these modifications are unknown (L'Italien, 1979; G.F.-L. Ames, 1979). Methylation of EF-Tu at K57 impedes GTP hydrolysis in vitro (Van Noort, 1986). Nutrient starvation promotes the conversion of N6-monomethyllysine to N6,N6-dimethyllysine at K57 in E. coli B EF-Tu (Young, 1990; Young, 1991). tufA encodes an essential function, with duplicate gene tufB, such that tufA or tufB can be deleted, but the double mutant is inviable. Coliphage Q beta replicase is comprised of the phage-encoded beta subunit and three bacterial proteins: TufB, Tsf and RpsA (Kondo, 1970; Kamen, 1970; Blumenthal, 1972; Wahba, 1974). RpsA is dispensible for RNA synthesis by coliphage Q beta replicase and is not part of the core replicase (Kamen, 1972; Hori, 1974; Landers, 1974). 50-80% of EF-Tu can be located at the cytoplasmic membrane, possibly as a result of nutrient stress, and EF-Tu may have a ribosome-independent role since it is present in at least a four-fold molar excess over ribosomes; methylation status of K57 may be related to membrane localization (Jacobson, 1976; Young, 1991). Various mutants and growth conditions have demonstrated that EF-Tu, or a precursor form pTu, can be localized to the outer membrane (Dombou, 1981; Lifson, 1986; Sedgwick, 1986). EF-Tu can form filamentous structures in vitro and has been suggested to be an actin-like cytoskeletal protein (Minkoff, 1975; Minkoff, 1976; Rosenbusch, 1976; Jacobson, 1976; Minkoff, 1977; Beck, 1978; Wurtz, 1978; Beck, 1979; Cremers, 1981; Schilstra, 1986; Helms, 1995; Helms, 1996; Norris, 2007). Although early results indicated a lack of an in vivo EF-Tu cytoskeletal structure in E. coli, subsequent experiments identified a helically organized EF-Tu-containing intracellular protofilament near the inner face of the cytoplasmic membrane with polysomes attached; it was suggested that an EF-Tu-containing cytoskeletal web might be the original prokaryotic cytoskeleton and that MreB evolved later to build upon the EF-Tu cytoplasmic network and be a cell shape determinant (Schilstra, 1984; Mayer, 2003; Mayer, 2006). In B. subtilis, EF-Tu is found in a static helical structure at the inner face of the cytoplasmic membrane co-localized with MreB; MreB and EF-Tu interact in vivo and in vitro; reduction of intracellular EF-Tu affects cell shape but not translation efficiency; EF-Tu intracellular protofilaments may serve as tracks for dynamic MreB shape-determining filaments (Defeu, 2010). HT_Cmplx23_Cyt: FusA+Tsf+TufA.HT_Cmplx4_Cyt: Tsf+TufA.

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BamHI EcoRI HindIII