Dipeptidase-C in Drosophila melanogaster: genetic, ontogenetic, and tissue-specific variation.
Dipeptidase-C in Drosophila melanogaster: genetic, ontogenetic, and tissue-specific variation.
复制标题
果蝇中的二肽酶-C:遗传、个体发生和组织特异性变异。
DOI:
10.1007/bf02399810
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发表时间:
1992
影响因子:
2.4
通讯作者:
Mathes,KD
中科院分区:
文献类型:
--
作者:
Hiraizumi,K;Hourani,CL;Zambarano,MC;Freeman4th,JE;Mathes,KD
Dip-A, Dip-B, andDip-Cconstitute structural genes for three peptidic enzymes inDrosophila melanogasterdistinct from the leucine aminopeptidases. Their ontogenetic and tissue distributions of activities suggest the involvement of these enzymes in a general metabolic role, such as the regulation of amino acid and oligopeptide pools to make amino acids available for protein synthesis. Screening of chromosome substitution isogenic lines for DIP-C activity indicated that, like DIP-A and DIP-B, unlinked activity modifiers exist forDip-C. The developmental profiles of dipeptidase activities are very similar, except in the pupal stage, during which DIP-C activity is markedly low compared to the other two enzymes. Intercorrelations of dipeptidase activities vary ontogenetically, which is consistent with the need for coordinate expression of these enzymes during certain developmental stages. Tissue-specific expressions of dipeptidases in larvae and adults are also similar, although the relative levels of DIP-A activity differ from those of DIP-B and DIP-C in certain organs and body parts. Some of the differences among chromosome substitution lines for dipeptidase activities appear to be systemic, while others are developmental stage-specific and tissue-specific. Second- and third-chromosome variants for DIP-C activity differed in their tissue distribution. This is consistent with the presence of temporal and spatial variants in natural populations for otherDrosophilaenzymes.