The Yeast ARGRII Regulatory Protein Has Homology with Various RNases and DNA Binding Proteins

Overview

Journal Mol Gen Genet

Specialties Genetics
Molecular Biology

Date 1988 Jan 1

PMID 3125409

Citations 10

Authors

F Messenguy

E Dubois

Affiliations

Soon will be listed here.

Abstract

Three regulatory proteins are involved in the post-transcriptional control of arginine metabolism in Saccharomyces cerevisiae: ARGRI, ARGRII and ARGRIII. The 880 amino acid ARGRII protein, like some DNA binding proteins, possesses in its N-terminal sequence a cysteine-rich region that presents homology to the zinc binding region of Escherichia coli aspartate transcarbamylase. ARGRII also has a region of 90 amino acids that is 30% homologous to the E. coli ARGR repressor. Moreover a 87 amino acid long sequence of ARGRII contains three stretches with significant homology to some viral, bacterial and pancreatic RNases. We propose a model in which the RNase-like sequence could regulate the expression of arginine anabolic messenger RNAs.

Citing Articles

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El Hajj Assaf C, Zetina-Serrano C, Tahtah N, El Khoury A, Atoui A, Oswald I Int J Mol Sci. 2020; 21(24).

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ArgRII, a component of the ArgR-Mcm1 complex involved in the control of arginine metabolism in Saccharomyces cerevisiae, is the sensor of arginine.

Amar N, Messenguy F, El Bakkoury M, Dubois E Mol Cell Biol. 2000; 20(6):2087-97.

PMID: 10688655 PMC: 110825. DOI: 10.1128/MCB.20.6.2087-2097.2000.

Transcriptional induction by aromatic amino acids in Saccharomyces cerevisiae.

Iraqui I, Vissers S, Andre B, Urrestarazu A Mol Cell Biol. 1999; 19(5):3360-71.

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Combinatorial regulation of the Saccharomyces cerevisiae CAR1 (arginase) promoter in response to multiple environmental signals.

Smart W, Coffman J, Cooper T Mol Cell Biol. 1996; 16(10):5876-87.

PMID: 8816501 PMC: 231589. DOI: 10.1128/MCB.16.10.5876.

Arginine-specific repression in Saccharomyces cerevisiae: kinetic data on ARG1 and ARG3 mRNA transcription and stability support a transcriptional control mechanism.

Crabeel M, LAVALLE R, Glansdorff N Mol Cell Biol. 1990; 10(3):1226-33.

PMID: 2406564 PMC: 361004. DOI: 10.1128/mcb.10.3.1226-1233.1990.

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