Trypanosomatidae: Isoleucine requirement and threonine deaminase in species with and without endosymbionts
Identifieur interne : 004051 ( Main/Exploration ); précédent : 004050; suivant : 004052Trypanosomatidae: Isoleucine requirement and threonine deaminase in species with and without endosymbionts
Auteurs : Silvia C. Alfieri [Brésil] ; E. Plessmann Camargo [Brésil]Source :
- Experimental Parasitology [ 0014-4894 ] ; 1981.
Abstract
Among the trypanosomatid protozoa (Crithidia fasciculata, Crithidia oncopelti, C. oncopelti aposymbiotic, Crithidia acanthocephali, Crithidia deanei, C. deanei aposymbiotic, Blastocrithidia culicis, B. culicis aposymbiotic, Leptomonas seymouri, Leptomonas collosoma, Herpetomonas samuelpessoai, Herpetomonas megaseliae, Herpetomonas muscarum muscarum, Herpetomonas mariadeanei, Phytomonas davidi, Endotrypanum schaudinni, Leishmania mexicana amazonensis, and Trypanosoma cruzi), biosynthetic threonine deaminase (l-threonine hydro-lyase (deaminating) EC 4.2.1.16) was found exclusively in species harboring symbionts: C. oncopelti, C. deanei, and B. culicis but not in other species examined nor in symbiont-free strains of symbiont-harboring species. By cell fractionation of C. deanei, a symbiont-rich subcellular fraction was isolated in which the specific activity of threonine deaminase was 10 times higher than that of crude homogenates. These results indicate that, in trypanosomatids, only species harboring a symbiont are capable of isoleucine synthesis and that threonine deaminase, the first enzyme of the isoleucine biosynthetic pathway, actually belongs to the symbiont. Species with symbionts do not require for growth either isoleucine or the metabolically related valine and leucine.
Url:
DOI: 10.1016/0014-4894(82)90080-7
Affiliations:
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<front><div type="abstract" xml:lang="en">Among the trypanosomatid protozoa (Crithidia fasciculata, Crithidia oncopelti, C. oncopelti aposymbiotic, Crithidia acanthocephali, Crithidia deanei, C. deanei aposymbiotic, Blastocrithidia culicis, B. culicis aposymbiotic, Leptomonas seymouri, Leptomonas collosoma, Herpetomonas samuelpessoai, Herpetomonas megaseliae, Herpetomonas muscarum muscarum, Herpetomonas mariadeanei, Phytomonas davidi, Endotrypanum schaudinni, Leishmania mexicana amazonensis, and Trypanosoma cruzi), biosynthetic threonine deaminase (l-threonine hydro-lyase (deaminating) EC 4.2.1.16) was found exclusively in species harboring symbionts: C. oncopelti, C. deanei, and B. culicis but not in other species examined nor in symbiont-free strains of symbiont-harboring species. By cell fractionation of C. deanei, a symbiont-rich subcellular fraction was isolated in which the specific activity of threonine deaminase was 10 times higher than that of crude homogenates. These results indicate that, in trypanosomatids, only species harboring a symbiont are capable of isoleucine synthesis and that threonine deaminase, the first enzyme of the isoleucine biosynthetic pathway, actually belongs to the symbiont. Species with symbionts do not require for growth either isoleucine or the metabolically related valine and leucine.</div>
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