In vivo and in vitro methylation of the elongation factor EF-Tu from Euglena gracilis chloroplast

Toledo, HÃ©ctor; Jerez, Carlos A.

doi:10.1016/0378-1097(90)90227-h

Cited by 2 publications

(2 citation statements)

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“…The elongation factor EF‐Tu is methylated in bacteria, Salmonella typhimurium and E. coli (Ames and Niakido, 1979; Ohba et al ., 1979; Toledo and Jerez, 1985); the elongation factor eEF1A is methylated in the fungus, Mucor (Hiatt et al ., 1982), in the protist E. gracilis chloroplast (Toledo and Jerez, 1990), in the brine shrimp Artemia salina (Amons et al ., 1983) and in the mammal, mouse (Coppard et al ., 1983), with E. coli EF‐Tu methylated at the single Lys56 position (L′Italien and Laursen, 1979). Interestingly, both the GTPase activity and the reactivity of the essential Cys81 residue are significantly less stimulated by tRNA when EF‐Tu is methylated (Van Noort et al ., 1986).…”

Section: Methylation Of Tfs and Hnrnp Proteinsmentioning

confidence: 99%

Methylation of proteins involved in translation

Polevoda¹,

Sherman²

2007

Molecular Microbiology

128

110

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SummaryMethylation is one of the most common protein modifications. Many different prokaryotic and eukaryotic proteins are methylated, including proteins involved in translation, including ribosomal proteins (RPs) and translation factors (TFs). Positions of the methylated residues in six Escherichia coli RPs and two Saccharomyces cerevisiae RPs have been determined. At least two RPs, L3 and L12, are methylated in both organisms. Both prokaryotic and eukaryotic elongation TFs (EF1A) are methylated at lysine residues, while both release factors are methylated at glutamine residues. The enzymes catalysing methylation reactions, protein methyltransferases (MTases), generally use S-adenosylmethionine as the methyl donor to add one to three methyl groups that, in case of arginine, can be asymetrically positioned. The biological significance of RP and TF methylation is poorly understood, and deletions of the MTase genes usually do not cause major phenotypes. Apparently methylation modulates intra-or intermolecular interactions of the target proteins or affects their affinity for RNA, and, thus, influences various cell processes, including transcriptional regulation, RNA processing, ribosome assembly, translation accuracy, protein nuclear trafficking and metabolism, and cellular signalling. Differential methylation of specific RPs and TFs in a number of organisms at different physiological states indicates that this modification may play a regulatory role.

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Section: Methylation Of Tfs and Hnrnp Proteinsmentioning

confidence: 99%

Methylation of proteins involved in translation

Polevoda¹,

Sherman²

2007

Molecular Microbiology

128

110

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“…It is possible that the absence of binding between eEF1α(1) and CSEP0064/BEC1054 in yeast is a false-negative result (Huang & Bader, 2009). If this were the case, it would indicate that other factors or posttranslational modification(s) of eEF1α(1) (Dever et al, 1989, Hiatt et al, 1982, L'Italien & Laursen, 1979, Ransom et al, 1998, Toledo & Jerez, 1990) not present in yeast are required for its association with CSEP0064/BEC1054. The specificity of the interaction with eEFα (1) is further underlined by the fact that the pairing CSEP0064/BEC1054-eEFA(3) yielded no detectable BiFC signal.…”

Section: Interactions Of Csep0064/bec1054 With Host Proteins and Rnamentioning

confidence: 99%

A fungal ribonuclease-like effector protein inhibits plant host ribosomal RNA degradation

Pennington

Jones

Kwon³

et al. 2018

Preprint

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KEY WORDSBlumeria graminis; effector protein; CSEP0064/BEC1054; RIP; Bimolecular Fluorescence Complementation; split YFP; RALPH; RNA-binding protein; RNase structure; powdery mildew Fungal RNase-like effector function -2 RALPH RNase-like proteins expressed in haustoria RFP red fluorescent protein RIP ribosome-inactivating protein RNase ribonuclease rRNA ribosomal RNA SRL sarcin-ricin loop Y2H yeast two-hybrid Fungal RNase-like effector function -3 3 ABSTRACT The biotrophic fungal pathogen Blumeria graminis causes the powdery mildew disease of cereals and grasses. Proteins with a predicted ribonuclease (RNase)-like fold (termed RALPHs) comprise the largest set of secreted effector candidates within the B. graminis f. sp. hordei genome. Their exceptional abundance suggests they play crucial functions during pathogenesis. We show that transgenic expression of RALPH CSEP0064/BEC1054 increases susceptibility to infection in monocotyledenous and dicotyledonous plants. CSEP0064/BEC1054 interacts in planta with five host proteins: two translation elongation factors (eEF1α and eEF1γ), two pathogenesis-related proteins (PR5 and PR10) and a glutathione-S-transferase.We present the first crystal structure of a RALPH, CSEP0064/BEC1054, demonstrating it has an RNase-like fold. The protein interacts with total RNA and weakly with DNA. Methyl jasmonate levels modulate susceptibility to aniline-induced host RNA fragmentation. In planta expression of CSEP0064/BEC1054 reduces the formation of this RNA fragment. We propose that CSEP0064/BEC1054 is a pseudoenzyme that binds to host ribosomes, thereby inhibiting the action of plant ribosome-inactivating proteins that would otherwise lead to host cell death, an unviable interaction and demise of the fungus.

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In vivo and in vitro methylation of the elongation factor EF-Tu from Euglena gracilis chloroplast

Cited by 2 publications

References 29 publications

Methylation of proteins involved in translation

Methylation of proteins involved in translation

A fungal ribonuclease-like effector protein inhibits plant host ribosomal RNA degradation

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