Two genes encoding putative mitochondrial alcohol dehydrogenases are present in the yeast Kluyveromyces lactis

Yeast - Tập 7 Số 4 - Trang 391-400 - 1991
Michele Saliola1, Roberta Gonnella1, Cristina Mazzoni1, Claudio Falcone1
1Department of Cell and Developmental Biology, University of Rome, ‘La Sapienza’ Città Universitaria, Piazzale A. Moro., 00185 Roma, Italy

Tóm tắt

Abstract

Four structural genes encoding isozymes of the alcohol dehydrogenase (ADH) system in the yeast Kluyveromyces lactis have been identified by hybridization to ADH2 DNA probes from Saccharomyces cerevisiae. In this paper we report on the isolation of KlADH4 and the complete sequencing of KlADH3 and KlADH4, two genes which show high homology to KlADH1, the ADH gene previously isolated in K. lactis, and to the ADH genes of S. cerevisiae. When compared with KlADH1, both KlADH3 and KlADH4 encode amino‐terminal extensions which show the characteristics of the mitochondrial targeting sequences. These extensions are poorly conserved both at the nucleotide and the amino acid level. Suprisingly, the KlADH4 extension shows a higher identity at the amino acid level to the one encoded by ADH3 of S. cerevisiae than to the KlADH3 presequence. KlADH3 and KlADH4, in contrast to the ADH3 gene of S. cerevisiae, show a strong bias in the choice of codons.

Từ khóa


Tài liệu tham khảo

10.1073/pnas.83.23.9011

10.1128/MCB.5.7.1743

10.1016/S0021-9258(19)81067-0

10.1007/BF00436877

10.1007/BF02428119

10.1007/BF00330840

10.1016/0022-2836(81)90181-9

Denis C. L., 1983, mRNA levels for the fermentative alcohol dehydrogenase of Saccharomyces cerevisiae decrease upon growth on a non fermentable carbon source, J. Biol. Chem., 25, 1165, 10.1016/S0021-9258(18)33174-0

10.1093/genetics/108.4.833

10.1038/332800a0

10.1093/nar/10.8.2625

10.1128/jb.172.7.3909-3917.1990

10.1093/nar/18.2.365

Ganzhorn A. J., 1987, Kinetic characterization of yeast alcohol dehydrogenases, J. Biol. Chem., 262, 3754, 10.1016/S0021-9258(18)61419-X

10.1016/0014-5793(88)81257-2

10.1002/j.1460-2075.1985.tb04111.x

10.1016/0304-4157(89)90002-6

10.1021/bi00404a009

10.1016/0378-1119(80)90054-2

10.1016/0003-9861(68)90487-6

Maniatis T., 1989, Molecular Cloning: a Laboratory Manual

Mooney D. T., 1990, Mutant alcohol dehydrogenase (ADH III) presequences that affect both in vitro mitochondrial import and in vitro processing by the matrix protease, Mol. Cell. Biol., 6, 2801

10.1128/MCB.6.1.70

10.1128/MCB.7.1.294

Russel P. R., 1983, The primary structure of the alcohol dehydrogenase gene from the fission yeast Schizosaccharmyces pombe, J. Biol. Chem., 258, 143, 10.1016/S0021-9258(18)33232-0

10.1002/yea.320060304

10.1073/pnas.74.12.5463

10.1128/MCB.6.6.1894

10.1093/nar/15.20.8573

10.1002/yea.320050106

Taguchi A. K. W., 1987, The identification and characterization of ADR6, a gene required for sporulation and for expression of the alcohol dehydrogenase II isozyme from S. cerevisiae, Genetics, 116, 523, 10.1093/genetics/116.4.523

10.1016/0092-8674(86)90846-9

van Loon A. P. G. M., 1986, Intracellular sorting of alcohol dehydrogenase isoenzyme in yeast: cytosolic location reflects absence of an aminoterminal targeting sequence for the mitochondrion, EMBO J., 5, 161, 10.1002/j.1460-2075.1986.tb04191.x

10.1002/j.1460-2075.1986.tb04364.x

10.1007/BF00391805

10.1093/nar/16.17.8714

10.1007/BF00329668

10.1128/MCB.5.11.3024