Abstract
Six leucine auxotrophic strains of the white rot basidiomycete Phanerochaete chrysosporium were characterized genetically and biochemically. Complementation studies involving the use of heterokaryons identified three leucine complementation groups. Since all of the leucine auxotrophs grew on minimal medium supplemented with α-ketoisocaproate as well as with leucine, the transaminase catalyzing the last step in the leucine pathway was apparently normal in all strains. Therefore, the wild-type, auxotrophic, and several heterokaryotic strains were assayed for the activities of the other enzymes specific to leucine biosynthesis. Leu2 and Leu4 strains (complementation group I) lacked only α-isopropylmalate synthase activity; Leu3 and Leu6 strains (group III) lacked isopropylmalate isomerase activity; and Leu1 and Leu5 strains (group II) lacked β-isopropylmalate dehydrogenase. Heterokaryons formed from leucine auxotrophs of different complementation groups had levels of activity for all three enzymes similar to those found in the wild-type strain.
Full text
PDF



Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Alic M., Gold M. H. Genetic Recombination in the Lignin-Degrading Basidiomycete Phanerochaete chrysosporium. Appl Environ Microbiol. 1985 Jul;50(1):27–30. doi: 10.1128/aem.50.1.27-30.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Eriksson K. E. Cellulases of fungi. Basic Life Sci. 1981;18:19–32. doi: 10.1007/978-1-4684-3980-9_3. [DOI] [PubMed] [Google Scholar]
- Glenn J. K., Gold M. H. Purification and characterization of an extracellular Mn(II)-dependent peroxidase from the lignin-degrading basidiomycete, Phanerochaete chrysosporium. Arch Biochem Biophys. 1985 Nov 1;242(2):329–341. doi: 10.1016/0003-9861(85)90217-6. [DOI] [PubMed] [Google Scholar]
- Gold M. H., Cheng T. M., Alic M. Formation, Fusion, and Regeneration of Protoplasts from Wild-Type and Auxotrophic Strains of the White Rot Basidiomycete Phanerochaete chrysosporium. Appl Environ Microbiol. 1983 Jul;46(1):260–263. doi: 10.1128/aem.46.1.260-263.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gold M. H., Cheng T. M. Induction of colonial growth and replica plating of the white rot basidiomycete Phanaerochaete chrysosporium. Appl Environ Microbiol. 1978 Jun;35(6):1223–1225. doi: 10.1128/aem.35.6.1223-1225.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gold M. H., Cheng T. M., Mayfield M. B. Isolation and Complementation Studies of Auxotrophic Mutants of the Lignin-Degrading Basidiomycete Phanerochaete chrysosporium. Appl Environ Microbiol. 1982 Oct;44(4):996–1000. doi: 10.1128/aem.44.4.996-1000.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gold M. H., Kuwahara M., Chiu A. A., Glenn J. K. Purification and characterization of an extracellular H2O2-requiring diarylpropane oxygenase from the white rot basidiomycete, Phanerochaete chrysosporium. Arch Biochem Biophys. 1984 Nov 1;234(2):353–362. doi: 10.1016/0003-9861(84)90280-7. [DOI] [PubMed] [Google Scholar]
- Gross S. R. The regulation of synthesis of leucine biosynthetic enzymes in Neurospora. Proc Natl Acad Sci U S A. 1965 Dec;54(6):1538–1546. doi: 10.1073/pnas.54.6.1538. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Renganathan V., Miki K., Gold M. H. Multiple molecular forms of diarylpropane oxygenase, an H2O2-requiring, lignin-degrading enzyme from Phanerochaete chrysosporium. Arch Biochem Biophys. 1985 Aug 15;241(1):304–314. doi: 10.1016/0003-9861(85)90387-x. [DOI] [PubMed] [Google Scholar]
- Ryan E. D., Kohlhaw G. B. Subcellular localization of isoleucine-valine biosynthetic enzymes in yeast. J Bacteriol. 1974 Nov;120(2):631–637. doi: 10.1128/jb.120.2.631-637.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ryan E. D., Tracy J. W., Kohlhaw G. B. Subcellular localization of the leucine biosynthetic enzymes in yeast. J Bacteriol. 1973 Oct;116(1):222–225. doi: 10.1128/jb.116.1.222-225.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Satyanarayana T., Umbarger H. E., Lindegren G. Biosynthesis of branched-chain amino acids in yeast: correlation of biochemical blocks and genetic lesions in leucine auxotrophs. J Bacteriol. 1968 Dec;96(6):2012–2017. doi: 10.1128/jb.96.6.2012-2017.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Smith M. H., Gold M. H. Phanerochaete chrysosporium beta-Glucosidases: Induction, Cellular Localization, and Physical Characterization. Appl Environ Microbiol. 1979 May;37(5):938–942. doi: 10.1128/aem.37.5.938-942.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ulm E. H., Böhme R., Kohlhaw G. Alpha-isopropylmalate synthase from yeast: purification, kinetic studies, and effect of ligands on stability. J Bacteriol. 1972 Jun;110(3):1118–1126. doi: 10.1128/jb.110.3.1118-1126.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]