Carbohydrates in mammalian tryptophanyl‐tRNA synthetase

Kovaleva, G. K.; Zheltova, A. O.; Nikitushkina, Tatyana V.; Egorov, Tsezi A.; Musoljamov, Aleksander Ch.; Kisselev, Lev L.

doi:10.1016/0014-5793(92)80802-n

Cited by 13 publications

(6 citation statements)

References 15 publications

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“…This phenomenon was confirmed in vivo by using human interferon-y-treated human ovarian cancer xenografts grown in nude mice [12]. Moreover, we have demonstrated that Trp-tRNA synthetase is a human autoantigen in some donors and cancer patients and this was hypothesized to be at least partially related to interferon induction Bovine pancreas Trp-tRNA synthetase is a glycoprotein [14] consisting of two subunits of about 60 kDa each [2]. Our previous studies have shown that it reaches high levels in bovine pancreas and comprises aproximately 3 % of the soluble protein fraction [15].…”

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confidence: 73%

A Mammalian Tryptophanyl‐tRNA Synthetase is Associated with Protein Kinase Activity

Paley

1997

European Journal of Biochemistry

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Bovine Trp-tRNA synthetase is a dimer with subunit molecular mass of 60 kDa (p60) which catalyzes ATP-dependent formation of tryptophanyl-tRNA. Evidence is presented that Trp-tRNA synthetase whose homogeneity had been proven by SDSPAGE and silver staining of the gel is autophosphorylated in vitro. Anti-(Trp-tRNA synthetase) antibodies, whose specificity was verified by using a combination of different approaches, were able to effectively inhibit and immunoprecipitate the Trp-tRNA-synthetase-associated kinase activity. The two-dimensional tryptic phosphopeptide map of autophosphorylated p60 Trp-tRNA synthetase was found to be similar to that of its major 40-kDa degradation fragment bearing resemblance to previously demonstrated unlabeled peptide patterns of the Trp-tRNA synthetase forms. Trp-tRNA synthetase which had undergone denaturation during SDS/PAGE, regained serinetthreonine specific protein kinase activity (PK 60) after guanidine treatment. Trp-tRNA synthetase induced phosphorylation of specific substrate such as 100-kDa protein in non-immune but not in anti-(Trp-tRNA synthetase) sera which distinguishes Trp-tRNA-synthetase-associated kinase from other protein kinases. Sequence analysis permitted the identification of regions of bovine Trp-tRNA synthetase sharing similarity with the catalytic domains of known protein kinases. These findings suggest that PK 60 and Trp-tRNA synthetase (p60) are either closely related or identical.Keywords: aminoacyl-tRNA synthetase from bovine pancreas ; autophosphorylation ; protein kinase ; histone.Aminoacyl-tRNA synthetases belong to an ancient protein family [I] and catalyze the esterification of a single amino acid to its cognate tRNA [ 2 ] . Based on a sequence and crystallographic structure, these enzymes are subdivided into two groups. Class I aminoacyl-tRNA synthetases share two consensus amino acid motifs, HIGH and KMSKS, while class I1 synthetases have another consensus region GLER 131.

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confidence: 73%

A Mammalian Tryptophanyl‐tRNA Synthetase is Associated with Protein Kinase Activity

Paley

1997

European Journal of Biochemistry

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“…The properties of placental hTrpRS and pancreatic bTrpRS seem to be very similar and possibly identical in terms of their putative subunit composition and kinetic parameters ; the size of the placental hTrpRS estimated by SDS/ PAGE is 58 kDa and the isoelectric point is 5.2 [43]. Highly purified bTrpRS is available [24,25,37,391, and recently hTrpRS (y2 protein) was purified (J. J. et al, unpublished data).…”

Section: Comparison Of Mammalian Trprs and Rf And Their Activitiesmentioning

confidence: 96%

“…bTrpRS was purified according to Kisselev et al [24] as modified by Kovaleva et al [25], and was kindly provided by G. Kovaleva. hTrpRS (y2 protein) was purified from interferon-y-induced human amnion cell cultures using chromatography on DEAE-cellulose and heparin-Sepharose columns [17] (and J. J., unpublished results).…”

Section: Trprs Purification and Assaymentioning

confidence: 99%

“…However by SDSPAGE and gel filtration, the molecular mass of bTrpRS was determined as 54 kDa [40] and as 58 5 2 kDa [41]. This difference in size could be due to post-translational modifications of the polypeptide chains, such as phosphorylation 131 -331, glycosylation [25] and possibly binding of lipids (A. Alesenko and G. Kovaleva, unpublished data). The native enzyme is a metalloprotein containing one Zn atom/ dimer, essential for structural integrity and catalytic activity [42].…”

Section: Comparison Of Mammalian Trprs and Rf And Their Activitiesmentioning

confidence: 99%

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Are the tryptophanyl‐tRNA synthetase and the peptide‐chain‐release factor from higher eukaryotes one and the same protein?

Frolova

Fleckner

Justesen

et al. 1993

European Journal of Biochemistry

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This close similarity between mammalian TrpRS and cloned RF is unexpected given the distinct functional properties of these proteins. Consequently, the question arises as to whether the mammalian TrpRS and RF activities reside on identical or very similar polypeptides. Alternatively, one may assume that the cloned rabbit cDNA encodes a protein other than rRF.Several properties (immunochemical, biochemical and physico-chemical) of mammalian TrpRS and RF have been compared. rTrpRS and rRF have distinct thermostability behaviours, and dissimilar chromatographic profiles on phosphocellulose. Both the anti-bTrpRS polyclonal antibodies and the monoclonal antibody Am2 strongly inhibit the bTrpRS and hTrpRS aminoacylation activities, but not the rRF activity. In addition, neither bTrpRS nor hTrpRS exhibit RF activity. It is concluded that (a) the functional centers responsible for the TrpRS and RF activities are structurally and functionally dissimilar and could hardly belong to the same protein domain; (b) RF and TrpRS probably reside on different polypeptide chains encoded by different genes, although it is still not excluded that the RF-and TrpRS-specific domains are situated on one and the same polypeptide chain; (c) the rabbit cDNA believed to encode RF, presumably encodes rTrpRS; this would explain why its deduced amino acid sequence has no similarity with bacterial RFs but is very similar to mammalian TrpRS.It has long been known that termination of translation is controlled by specific components of the protein-synthesizing machinery, including termination codons in the

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“…WRS purification and assay Bovine WRS was purified according to Kisselev et al (1979) as modified by Kovaleva et al (1992), and was kindly provided by G.Kovaleva. The WRS activity was measured by tryptophanylation of yeast tRNA enriched in tRNATrp (kindly provided by G.Keith) according to Kisselev et al (1979).…”

Section: Release Assaymentioning

confidence: 99%

Mammalian polypeptide chain release factor and tryptophanyl-tRNA synthetase are distinct proteins.

et al. 1993

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A very high (approximately 90%) structural similarity exists between the bovine, human and murine tryptophanyl‐tRNA synthetases (WRS), and quite unexpectedly the rabbit polypeptide chain release factor (eRF). This similarity may point to a very close resemblance or identity between these proteins involved in distinct steps of protein synthesis, or inadvertently to an incorrect assignment of the clone reported to encode eRF, since the structure of clones encoding WRS were confirmed by peptide sequencing. Using high resolution column chromatography and sucrose gradient centrifugation combined with assays for WRS and eRF activities, we show that functionally distinct WRS and eRF proteins can be completely separated from each other. Moreover, a putative anti‐eRF monoclonal antibody appears incapable of immunoprecipitating the eRF activity or binding to protein(s) possessing eRF activity. This antibody binds to protein fractions which coincide in various separation procedures with rabbit WRS activity, and to pure bovine WRS. The protein expressed in Escherichia coli from the original cDNA clone initially reported to encode eRF, has WRS activity but not eRF activity. Resequencing of the fragment of the original rabbit cDNA demonstrates the presence of the previously overlooked HXGH motif typical of class I aminoacyl‐tRNA synthetases. Consequently, mammalian WRS and eRF are different proteins, and the cDNA clone formerly assigned as encoding eRF encodes rabbit WRS.

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Carbohydrates in mammalian tryptophanyl‐tRNA synthetase

Cited by 13 publications

References 15 publications

A Mammalian Tryptophanyl‐tRNA Synthetase is Associated with Protein Kinase Activity

A Mammalian Tryptophanyl‐tRNA Synthetase is Associated with Protein Kinase Activity

Are the tryptophanyl‐tRNA synthetase and the peptide‐chain‐release factor from higher eukaryotes one and the same protein?

Mammalian polypeptide chain release factor and tryptophanyl-tRNA synthetase are distinct proteins.

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