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A M Rodríguez-Torres

Publications and source records attributed to A M Rodríguez-Torres.

6 recordsLinked to original sources
PubMed1999

Disruption of six novel Saccharomyces cerevisiae genes reveals that YGL129c is necessary for growth in non-fermentable carbon sources, YGL128c for growth at low or high temperatures and YGL125w is implicated in the biosynthesis of methionine.

Six open reading frames (ORFs) from chromosome, VII, YGL131c, YGL129c, YGL128c, YGL125w, YGL124c and YGL121c, were disrupted by deletion cassettes with short flanking regions homologous to the target locus (SFH). YGL129c is necessary for growth in non-fermentable carbon sources, YGL128c for growth at low or high temperatures and YGL125w is implicated in the biosynthesis of methionine. With regard to the other ORFs, basic phenotypic analyses did not reveal any significant clues about their function.

Carbon↗
PubMed1996

PICDI, a simple program for codon bias calculation.

PICDI is a very simple program designed to calculate the Intrinsic Codon Deviation Index (ICDI). The program is available in Macintosh as well a PC format. Requirements for correct input of the sequences have been kept to a minimum and the analysis of sequences up to 2000 codons is very quick. The ICDI is very useful for estimation of codon bias of genes from species in which optimal codons are not known. The availability of a computer program for its calculation will increase its usefulness in the fields of Molecular Biology and Biotechnology.

Codon↗
PubMed1995

Yeast phylogenetic relationships based on cytochrome c sequences.

The availability of the KICYC1 sequence was used to establish homologies with other cytochrome c genes from yeasts and the fungus Neurospora crassa. In terms of nucleotide composition, the cytochrome c gene from Kluyveromyces lactis showed a higher homology with Schwanniomyces occidentalis than with Saccharomyces cerevisiae, and this point is discussed in regard to the differences found in the codon usage of these yeasts. The deduced amino acidic composition of the protein facilitated comparison of its sequence with other cytochrome c protein sequences and new assignments of phylogenetic relationships. In this context Kluyveromyces lactis was most closely related to Candida krusei.

Cytochrome c Group↗
PubMed1994

Codon usage in Kluyveromyces lactis and in yeast cytochrome c-encoding genes.

Codon usage (CU) in Kluyveromyces lactis has been studied. Comparison of CU in highly and lowly expressed genes reveals the existence of 21 optimal codons; 18 of them are also optimal in other yeasts like Saccharomyces cerevisiae or Candida albicans. Codon bias index (CBI) values have been recalculated with reference to the assignment of optimal codons in K. lactis and compared to those previously reported in the literature taking as reference the optimal codons from S. cerevisiae. A new index, the intrinsic codon deviation index (ICDI), is proposed to estimate codon bias of genes from species in which optimal codons are not known; its correlation with other index values, like CBI or effective number of codons (Nc), is high. A comparative analysis of CU in six cytochrome-c-encoding genes (CYC) from five yeasts is also presented and the differences found in the codon bias of these genes are discussed in relation to the metabolic type to which the corresponding yeasts belong. Codon bias in the CYC from K. lactis and S. cerevisiae is correlated to mRNA levels.

Amino Acids↗
PubMed1987

[Characterization of an inhibitor of glucose-6-phosphate dehydrogenase].

A strong inhibitor of G6PDH has been detected in rat liver homogenates. The inhibitor, isolated by ultrafiltration methods, proved to be very stable under incubation with trypsin and high temperatures. Gel-filtration through Sephadex G-75 showed it to have a molecular weight of 3,500 daltons, though perchloric acid treatment produced a light form of 900 daltons. Both forms of inhibitor act as competitive inhibitor with respect to G6P and exhibit non-competitive inhibition pattern with respect to NADP+. Physical and kinetic properties, and the increase of G6PDH activity at low NADP+ concentrations, in the presence of NADPH and inhibitor or palmitoyl-CoA, in relation to the G6PDH activity in presence of NADPH, lead to the identification of the low-molecular weight inhibitor as palmitoyl-CoA.

Acyl Coenzyme A↗