Purification and properties of methionyl‐tRNA‐synthetase from yellow lupine seeds

Joachimiak, Andrzej; Barciszewski, Jan; Twardowski, Tomasz; Barciszewska, Mirosława Z.; Wiewiórowski, M.

doi:10.1016/0014-5793(78)80802-3

Cited by 24 publications

(5 citation statements)

References 11 publications

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“…Rice MetRS form a dimer structure at higher concentrations (22). We obtained similar results earlier for MetRS from Lupinus luteus (lupin), which formed dimers and also higher-order multimers (24). However, because rice MetRS lacking a C-terminal extension is a monomer regardless of concentration, it is conceivable that the EMAP II-like domain participates directly in a dimer formation.…”

Section: Resultssupporting

confidence: 87%

Swapping of Three‐Dimensional Domains as a Molecular Mechanism of Dimerization of Aminoacyl‐tRNA Synthetases

Deniziak

Barciszewski

2002

IUBMB Life

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SummaryIt has been shown recently that many proteins undergo oligomerization through exchange of structural elements. That process, termed a 3D domain swapping, is the replacement of a portion of the tertiary structure of a protein with an identical piece from a second polypeptide chain. When the exchange is reciprocated, domain-swapped dimers embrace with the exchange of elements of secondary structure or domains; however, if the exchange is not reciprocated but propagated along multiple polynucleotide chains, higher-order assemblies may form. In this paper we discuss swapping as a general mechanism of aminoacyl-tRNA synthetases dimerization, specifically plant methionyl-tRNA synthetase.IUBMB Life, 54: 85-88, 2002

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Section: Resultssupporting

confidence: 87%

Swapping of Three‐Dimensional Domains as a Molecular Mechanism of Dimerization of Aminoacyl‐tRNA Synthetases

Deniziak

Barciszewski

2002

IUBMB Life

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“…The Km value of 32 /LM obtained for methionine is similar to the value reported for the methionyl-tRNA synthetase from E. coli (23), wheat germ (25), and yellow lupin seeds (17) but is 1 order of magnitude lower than the value reported for S. lutea (14) and rat liver (8,9). The enzyme was similar to other methionyl-tRNA synthetases in having an absolute requirement for Mg2+ ions, having an optimum Mg/ATP ratio and being sensitive to sulfhydryl-group reagents.…”

Section: Discussionsupporting

confidence: 82%

“…The molecular weight of peak I was twice the value obtained for the methionyl-tRNA synthetase from E. coli (18), wheat germ (10), and lupin seeds (17). The molecular weight of peak II was similar to the molecular weight of the protein band obtained by SDS-polyacrylamide gel electrophoresis of wheat germ methionyl-tRNA synthetase (25).…”

Section: Discussionsupporting

confidence: 58%

Methionyl-tRNA Synthetase from Phaseolus aureus: Purification and Properties

Burnell¹

1981

Plant Physiol.

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“…The Km for ATP was calculated to be 1.18 mt; this value is of the same order of magnitude as the value obtained for the methionyl-tRNA synthetase from Sarcina lutea (15) but is higher than the Km value obtained for Paracoccus denitrfifcans (11), lupin seeds (20), and rat liver (12 Exchange than the Km (sulfate) but the V,,,x (selenate) was 3-fold less than the Vmax (sulfate). The enzyme kinetics of the effect of selenate on sulfate-dependent ATP-PPi exchange was consistent with both substrates competing for a single site (29) (Fig.…”

Section: Hydroxyapatite Column Chromatographymentioning

confidence: 81%

Selenium Metabolism in Neptunia amplexicaulis

Burnell¹

1981

Plant Physiol.

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ATP sufurylase (EC 2.7.7.4), cysteinyl-tRNA synthetase (EC 6.1.1.16), and methlonyl-tRNA synthetase (EC 6.1.1.10) from Administration of selenate to a variety of plants and microorganisms results in the appearance of selenium in various amino acids, peptides, and proteins (19). These studies led to the conclusion that selenate was metabolized via the assimilatory sulfate reduction pathway. This was supported by reports that yeast ATP sulfurylase catalyzed the synthesis of adenosine 5'-phosphoselenate from selenate (13). Shaw and Anderson (32) also reported that spinach leaf ATP sulfurylase catalyzed selenate-dependent ATPPPi exchange. Further support for the above proposal has been provided by a number of reports that the cysteine synthetase from bacteria (10) and both selenium-accumulating and nonaccumulating plants (22) utilize sulfide and selenide for the synthesis of cysteine and selenocysteine, respectively. Finally, a number of studies with both plants and microorganisms have shown that methionyl-tRNA synthetase (3,11,15,16, 25) and cysteinyl-tRNA synthetase (8,9,11,12, 40) can use the corresponding selenium analogs as substrates.There is now growing evidence to indicate that there are parts ofthe assimilatory sulfate reduction pathway from which selenium is excluded. Shaw and Anderson (34) reported that purified ATP sulfurylase from both selenium-accumulators and nonaccumulators could synthesize adenosine 5'-phosphosulfate from ATP and sulfate, but they were unable to synthesize adenosine 5'-phosphoselenate from ATP and selenate. Burnell and Whatley (9) This paper reports that purified ATP sulfurylase from Neptunia amplexicaulis (a selenium-accumulator) catalyzes the synthesis of adenosine 5'-phosphoselenate, that crude extracts catalyze the synthesis of 3'-phosphoadenosine 5'-phosphosulfate but do not catalyze the synthesis of 3'-phosphoadenosine 5'-phosphoselenate, and that purified cysteinyl-and methionyl-tRNA synthetase are unable to distinguish between sulfate-containing substrates and the selenium-containing analogs.A mechanism for the exclusion of selenium-containing amino acids from incorporation into proteins is proposed, together with a pathway for selenium metabolism in N. amplexicaulis. MATERIALS AND METHODS PLANT MATERIALSSeeds of N. amplexicaulis F. richmondii (family, Mimosaceae) were collected from seleniferous areas of Northwest Queensland, Australia. Seeds were scored with a razor blade to render the hard seed coat permeable to water and germinated on filter paper soaked in water, and the seedlings were raised in a glasshouse.

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Purification and properties of methionyl‐tRNA‐synthetase from yellow lupine seeds

Cited by 24 publications

References 11 publications

Swapping of Three‐Dimensional Domains as a Molecular Mechanism of Dimerization of Aminoacyl‐tRNA Synthetases

Swapping of Three‐Dimensional Domains as a Molecular Mechanism of Dimerization of Aminoacyl‐tRNA Synthetases

Methionyl-tRNA Synthetase from Phaseolus aureus: Purification and Properties

Selenium Metabolism in Neptunia amplexicaulis

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