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Effects of lysine, threonine and methionine on light-driven protein synthesis in isolated pea (Pisum sativum L.) chloroplasts

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Abstract

Light-driven incorporation of [14C]leucine (LEU) into protein in isolated pea chloroplasts was inhibited by 0.1 and 1 mM lysine (LYS), 0.1–10 mM threonine (THR) and 1 mM methionine (MET). Equimolar combinations of LYS plus THR were inhibitory at both 0.1 and 0.5 mM. Incorporation of [14C] aspartic acid (ASP) and [3H]tyrosine (TYR) was also reduced by 1 mM LYS or THR. In the cases tested, LYS and/or THR inhibitions were partially or fully reversed by 0.1 mM MET. [35S]MET incorporation was unaffected or stimulated by LYS and THR. These data are consistent with the hypothesis that MET is biosynthesized in isolated chloroplasts and that its synthesis is regulated by LYS and/or THR. Of 16 other amino acids tested at 1 mM, isoleucine, phenylalanine, tryptophan, tyrosine and valine inhibited protein synthesis.

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Abbreviations

DCMU:

3-(3,4-dichlorophenyl)-1,1-dimethylurea

ASP:

aspartic acid

HS:

homoserine

ILE:

isoleucine

LEU:

leucine

LYS:

lysine

MET:

methionine

THR:

threonine

TYR:

tyrosine

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Author notes

  1. W. Ronald Mills

    Present address: Biochemistry Department, Rothamsted Experimental Station, AL5 2JQ, Harpenden, Herts, UK

Authors and Affiliations

  1. Department of Botany, Miami University, 45056, Oxford, OH, USA

    W. Ronald Mills & Kenneth G. Wilson

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  1. W. Ronald Mills
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  2. Kenneth G. Wilson
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Additional information

A portion of this work was included in the Doctoral Dissertation of W.R.M. (Mills, 1977)

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Ronald Mills, W., Wilson, K.G. Effects of lysine, threonine and methionine on light-driven protein synthesis in isolated pea (Pisum sativum L.) chloroplasts. Planta 142, 153–160 (1978). https://doi.org/10.1007/BF00388206

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  • DOI: https://doi.org/10.1007/BF00388206

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