Characterization of protoporphyrin as the physiological regulator of delta-aminolevulinate dehydratase in Neurospora crassa

Chandrika, SR and Kumar, C Chandra and Padmanaban, G (1980) Characterization of protoporphyrin as the physiological regulator of delta-aminolevulinate dehydratase in Neurospora crassa. In: Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 607 (2). pp. 331-338.

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Abstract

In Neurospora crassa, the activity of δ-aminolevulinate dehydratase, the second and rate-limiting enzyme of the heme-biosynthetic pathway, is low in normal cells compared to the activity detected in plants, animals and bacteria. The activity is almost undetectable when Neurospora crassa is grown under iron-deficient conditions. The enzyme activity increases strikingly on addition of iron to iron-deficient cultures. This increase can be blocked by the addition of protoporphyrin, the penultimate product of the heme-biosynthetic pathway, to the cultures. The question whether iron directly acts at the genetic level or acts merely by removing protoporphyrin, converting the latter into heme prosthetic groups of hemoproteins, has been investigated by studying the effect of inhibition of heme synthesis on the induction of δ-aminolevulinate dehydratase. It has been found that treatments with levulinic acid or cyanide which inhibit the formation of the porphyrin moiety, induce δ-aminolevulinate dehydratase, whereas treatments which inhibit at a step after protoporphyrin formation (iron-deficiency and cobalt treatment) repress the enzyme. The endogenous levels of protoporphyrin are strictly controlled: a decrease below the optimum level causing induction and an increase above the optimum level leading to repression of δ-aminolevulinate dehydratase. Levulinic acid and cyanide can induce the enzyme in iron-deficient cultures in the absence of added iron, indicating that the metal iron acts only by converting protoporphyrin to heme fixed in hemoproteins in Neurospora crassa. Therefore it is suggested that protoporphyrin is the physiological regulator of δ-aminolevulinate dehydratase in Neurospora crassa.

Item Type:	Journal Article
Publication:	Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis
Publisher:	Elsevier Science
Additional Information:	Copyright of this article belongs to Elsevier Science.
Keywords:	Protoporphyrin;Enzyme induction;Enzyme repression; δ-Aminolevulinate dehydratase;Heme biosynthesis;(Neurospora crassa).
Department/Centre:	Division of Biological Sciences > Biochemistry
Date Deposited:	19 Aug 2009 06:34
Last Modified:	19 Sep 2010 05:41
URI:	http://eprints.iisc.ac.in/id/eprint/22391

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