The effects of selected nitrogen compounds on the growth of plant tissue cultures

Steward, F. C.; Pollard, J.K.; Patchett, Arthur A.; Witkop, B.

doi:10.1016/0006-3002(58)90477-3

Cited by 74 publications

(17 citation statements)

References 11 publications

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“…This inhibitory action was reversed when proline was supplied simultaneously, and the different degrees of growth inhibition observed in the various plant species could be explained by differences in their endogenous proline concentration. Azetidine-2-carboxylic acid therefore forms a potent proline analogue and similar growth inhibitions have been reported in carrot-tissue cultures, Escherichia coli and chick embryos (Steward, Pollard, Patchett & Witkop, 1958;Fowden & Richmond, 1963;.…”

supporting

confidence: 62%

Purification, properties and comparative specificities of the enzyme prolyl-transfer ribonucleic acid synthetase from Phaseolus aureus and Polygonatum multiflorum

Peterson

Fowden

1965

Biochemical Journal

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1. A prolyl-s-RNA synthetase (prolyl-transfer RNA synthetase) has been purified about 250-fold from seed of PhaseoluB aureus (mung bean), a species not producing azetidine-2-carboxylic acid, and more than 10-fold from rhizome apices of Polygonatum multiflorum, a liliaceous species containing azetidine-2-carboxylic acid. The latter enzyme was unstable during ammonium sulphate fractionation. 2. The enzymes exhibited different substrate specificities towards the analogue. That from Phaseolus, when assayed by the ATP-PP1 exchange, showed azetidine-2-carboxylic acid activation at about one-third the rate with proline. Both labelled imino acids gave rise to a labelled aminoacyl-s-RNA. The enzyme fromPolygonatum, however, activated only proline. 3. The enzyme from Polygonatum also formed a labelled prolyl-s-RNA with Pha8eolu8 s-RNA but at a lower rate than when the Phaseolu8 enzyme was used. No reaction occurred when the Phaseolus enzyme was coupled with Polygonatum s-RNA, and only a very slight one was observed when both enzyme and s-RNA came from Polygonatum. 4. Protein preparations from seeds of Pisum sativum, another species not producing azetidine-2-carboxylic acid, also activated the analogue in addition to proline, whereas those from rhizome and seeds of Convallaria, the species from which the analogue was originally isolated, failed to activate it. However, a liliaceous species not producing the analogue, Asparagus officinalis, activated it. 5. Of the other proline analogues investigated, only 3,4-dehydro-DL-proline and L-thiazolidine-4-carboxylic acid were active with the enzyme preparation from Pha8eolus. 6. pH optima of 7*9 and 8-4 were established for the enzymes from Phaseolu,s and Polygonatum respectively. 7. The Phaseolus enzyme was specific for ATP and PPi. Mn2+ partially replaced the requirement for Mg2+ as cofactor. Preincubation with p-chloromercuribenzoate at a concentration of 0 5mM or higher produced over 99% inhibition ofthePhaseolus enzyme. One-half the enzymic activity was destroyed by preheating for 5min. at 620 in tris-hydrochloric acid buffer, pH7.9. 8. All experimental evidence supports the hypothesis that azetidine-2-carboxylic acid and proline are activated by the same enzyme in Phaseolus preparations, whereas the analogue was inactive in all Polygonatum preparations. The possible nature of this different substrate behaviour is discussed.

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supporting

confidence: 62%

Purification, properties and comparative specificities of the enzyme prolyl-transfer ribonucleic acid synthetase from Phaseolus aureus and Polygonatum multiflorum

Peterson

Fowden

1965

Biochemical Journal

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“…The inhibition of growth by the hydroxyprolines can be almost completely reversed by free proline (5,13,29). If the in'hibition of protein-bound hydroxyproline formation is related to the growth illhibition, one would expect free proline to prevenlt this inhibition.…”

Section: Resultsmentioning

confidence: 99%

“…In the absence of auxin, free hydroxyproline exerts little or no inhibition of hydroxyproline formnation. Furtherore free hydroxyproline has no effect on respirtion, RNA synthesis or the incorporation of leucine into protein.Hydroxyproline is not a general inhibitor of metabolism or protein synthesis in Avena coleoptiles.These results suggest that free hydroxyproline may inhibit auxin-induced cell elongation by blocking the formation or utilization of a particular hydroxyproline-rich protein which must be incorporated into the cell wall during auxin-induced wall extension.Free hydroxyproline is an effective inhibitor of auxin-induced growth in Avena coleoptile (5, 7.19) and a variety of callus tissues (13,16,29). The ability of free pgoline to completely reverse this inhibition (5,13,19,29) suggests that hydroxyproline is acting as an antagonist of some facet of proline metabolism.…”

mentioning

confidence: 99%

“…Free hydroxyproline is an effective inhibitor of auxin-induced growth in Avena coleoptile (5, 7.19) and a variety of callus tissues (13,16,29). The ability of free pgoline to completely reverse this inhibition (5,13,19,29) suggests that hydroxyproline is acting as an antagonist of some facet of proline metabolism.…”

mentioning

confidence: 99%

“…The ability of free pgoline to completely reverse this inhibition (5,13,19,29) suggests that hydroxyproline is acting as an antagonist of some facet of proline metabolism. Since most amino acid antagonists exert their effect on some aspect of protein synthesis (26), it was suggested (5) that free hydroxyproline inhibits growth by interfering with the synthesis of some protein which is essential for cell elongation.…”

mentioning

confidence: 99%

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Inhibition of Formation of Protein-Bound Hydroxyproline by Free Hydroxyproline in Avena Coleoptiles

Cleland¹

1967

Plant Physiol.

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Summary. Free hydroxyproline inhibits the formation of protein-bound hydroxyproline from proline to a considerably greater extent than it does the incorporation of proline into prbtein of auxin-treated Avena coleoptiles. This inhibition is greater in the wall th!an in the cytoplasmic fraction. In the absence of auxin, free hydroxyproline exerts little or no inhibition of hydroxyproline formnation. Furtherore free hydroxyproline has no effect on respirtion, RNA synthesis or the incorporation of leucine into protein.Hydroxyproline is not a general inhibitor of metabolism or protein synthesis in Avena coleoptiles.These results suggest that free hydroxyproline may inhibit auxin-induced cell elongation by blocking the formation or utilization of a particular hydroxyproline-rich protein which must be incorporated into the cell wall during auxin-induced wall extension.Free hydroxyproline is an effective inhibitor of auxin-induced growth in Avena coleoptile (5, 7.19) and a variety of callus tissues (13,16,29). The ability of free pgoline to completely reverse this inhibition (5,13,19,29) suggests that hydroxyproline is acting as an antagonist of some facet of proline metabolism. Since most amino acid antagonists exert their effect on some aspect of protein synthesis (26), it was suggested (5) that free hydroxyproline inhibits growth by interfering with the synthesis of some protein which is essential for cell elongation. Available evidence was not sufficienit, lhowever, to rule out the possibility that hydroxylproline is a general metabolic inhibitor.The purpose of this investigation was to examine the effects of hydroxyproline on several aspects of the metabolism of Avena coleoptile tissues and, in particular, to determine its effects on protein synthesis. Since allohvdroxyproline is mre effective than hydroxyproline as a growth inhibitor (7), it was also included in this gtudy. It will be shown lhere that the 2 hydroxyprolines exert a specific inhibition of one facet of protein synthesis, the formation from proline of protein-bound hydroxyproline.1 Supported bv Grant GM-12881 from the United States Public Health Service and Grant GB-5385X from the National Science Foundation. Materials and MethodsThe plant material consisted of 5 or 14 mm sections cut from 25 to 32 mm coleoptiles of Avena sativa, var. Victorv. Seedlings were grown and sections prepared as detailed earlier (3). rhe primary leaf was removed from all sections. L-Proline, hydroxyproline (4-trans-hydroxy-L-proline), and allohydroxyprol;ine (4-cis-hydroxy-L-proline) were obtained from California Corporation for Biochemical Research. L-Proline-u-14C (200 mc/ mmole) and DL-leucine-1-l"C (4 mc/mmole), were from New England Nuclear Corporation. Hydroxyproline and allohydroxyproline were used at concentrations (1 and 0.5 mm, respectively) which caused maximal inhibition of auxin-induced growth (7).IAA was used at 5 jig/ml.Oxygen; uptake was determined by the standard Warburg manometric techniques with groups of thirty 5 mm sections in 2.7 ml of basal medium (2.5...

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Toxic Amino Acids: Their Action as Antimetabolites

Fowden¹,

Lewis²,

Tristram³

1967

Advances in Enzymology - And Related Areas of Molecular Biology

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The effects of selected nitrogen compounds on the growth of plant tissue cultures

Cited by 74 publications

References 11 publications

Purification, properties and comparative specificities of the enzyme prolyl-transfer ribonucleic acid synthetase from Phaseolus aureus and Polygonatum multiflorum

Purification, properties and comparative specificities of the enzyme prolyl-transfer ribonucleic acid synthetase from Phaseolus aureus and Polygonatum multiflorum

Inhibition of Formation of Protein-Bound Hydroxyproline by Free Hydroxyproline in Avena Coleoptiles

Toxic Amino Acids: Their Action as Antimetabolites

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