Mutations in an Abf1p binding site in the promoter of yeast RPO26 shift the transcription start sites and reduce the level of RPO26 mRNA

Nouraini, Shahrzad; Mcbroom, L. D. B.; Friesen, James D.

doi:10.1002/(sici)1097-0061(199610)12:13<1339::aid-yea31>3.0.co;2-c

Cited by 5 publications

(1 citation statement)

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“…Little is known about the mechanisms that confer different temperature-dependent phenotypes. Research done on lower organisms like bacteria (Tamai et al 1998) and yeast (Nouraini et al 1996) and in plants (Gilmour et al 1998;Zhu et al 2007) has shown that mutations in the cis-regulatory region show temperature-dependent phenotypes. Work done on the W3133 operon in bacteria showed that an insertional mutation in the promoter region could confer a temperature-sensitive phenotype and affect transcription efficiency by stabilizing the DNA stem loop structure (Tamai et al 1998).…”

Section: Discussionmentioning

confidence: 99%

A cis-Regulatory Mutation in Troponin-I of Drosophila Reveals the Importance of Proper Stoichiometry of Structural Proteins During Muscle Assembly

et al. 2015

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Rapid and high wing-beat frequencies achieved during insect flight are powered by the indirect flight muscles, the largest group of muscles present in the thorax. Any anomaly during the assembly and/or structural impairment of the indirect flight muscles gives rise to a flightless phenotype. Multiple mutagenesis screens in Drosophila melanogaster for defective flight behavior have led to the isolation and characterization of mutations that have been instrumental in the identification of many proteins and residues that are important for muscle assembly, function, and disease. In this article, we present a molecular-genetic characterization of a flightless mutation, flightless-H (fliH), originally designated as heldup-a (hdp-a). We show that fliH is a cis-regulatory mutation of the wings up A (wupA) gene, which codes for the troponin-I protein, one of the troponin complex proteins, involved in regulation of muscle contraction. The mutation leads to reduced levels of troponin-I transcript and protein. In addition to this, there is also coordinated reduction in transcript and protein levels of other structural protein isoforms that are part of the troponin complex. The altered transcript and protein stoichiometry ultimately culminates in unregulated acto-myosin interactions and a hypercontraction muscle phenotype. Our results shed new insights into the importance of maintaining the stoichiometry of structural proteins during muscle assembly for proper function with implications for the identification of mutations and disease phenotypes in other species, including humans.

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