Comparison of the mitochondrial endonucleases from Neurospora crassa and Saccharomyces cerevisiae

1985 ◽  
Vol 31 (7) ◽  
pp. 654-656 ◽  
Author(s):  
Richard G. von Tigerstrom ◽  
Sheilah Stelmaschuk
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Neurospora Crassa ◽  
Mode Of Action ◽  
Elevated Temperatures ◽  
Physiological Role ◽  
Intracellular Location ◽  
Substrate Specificities ◽  
Structural Differences ◽  
Specific Activities

The endonucleases from Neurospora crassa and Saccharomyces cerevisiae are not closely related antigenically. They also differ with respect to their activity at pH 8, their degree of hydrophobicity, and their sensitivity to elevated temperatures. However, the two nucleases have similar specific activities, are inhibited by EDTA, and have nearly identical substrate specificities. Since the enzymes also have the same mode of action and intracellular location, these similarities may indicate that they have the same physiological role despite their structural differences.

scholarly journals Yeast Isw1p Forms Two Separable Complexes In Vivo

2003 ◽  
Vol 23 (1) ◽  
pp. 80-91 ◽  
Author(s):  
Jay C. Vary, ◽  
Vamsi K. Gangaraju ◽  
Jun Qin ◽  
Carolyn Church Landel ◽  
Charles Kooperberg ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Transcriptional Regulation ◽  
Chromatin Remodeling ◽  
Elevated Temperatures ◽  
Cellular Processes ◽  
Biochemical Assays ◽  
Associated Proteins ◽  
Chromatin Remodeling Complexes ◽  
Specific Activities

ABSTRACT There are several classes of ATP-dependent chromatin remodeling complexes, which modulate the structure of chromatin to regulate a variety of cellular processes. The budding yeast, Saccharomyces cerevisiae, encodes two ATPases of the ISWI class, Isw1p and Isw2p. Previously Isw1p was shown to copurify with three other proteins. Here we identify these associated proteins and show that Isw1p forms two separable complexes in vivo (designated Isw1a and Isw1b). Biochemical assays revealed that while both have equivalent nucleosome-stimulated ATPase activities, Isw1a and Isw1b differ in their abilities to bind to DNA and nucleosomal substrates, which possibly accounts for differences in specific activities in nucleosomal spacing and sliding. In vivo, the two Isw1 complexes have overlapping functions in transcriptional regulation of some genes yet distinct functions at others. In addition, these complexes show different contributions to cell growth at elevated temperatures.

scholarly journals High yield expression of the Neurospora crassa plasma membrane H(+)-ATPase in Saccharomyces cerevisiae

1994 ◽  
Vol 269 (26) ◽  
pp. 17705-17712
Author(s):  
S.K. Mahanty ◽  
U.S. Rao ◽  
R.A. Nicholas ◽  
G.A. Scarborough
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Plasma Membrane ◽  
Neurospora Crassa ◽  
High Yield

scholarly journals Analysis of thepdx-1(snz-1/sno-1) Region of theNeurospora crassaGenome: Correlation of Pyridoxine-Requiring Phenotypes With Mutations in Two Structural Genes

Genetics ◽  
2001 ◽  
Vol 157 (3) ◽  
pp. 1067-1075 ◽  
Author(s):  
Laura E Bean ◽  
William H Dvorachek ◽  
Edward L Braun ◽  
Allison Errett ◽  
Gregory S Saenz ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Stationary Phase ◽  
Neurospora Crassa ◽  
Vitamin B6 ◽  
Structural Genes ◽  
Protein Coding ◽  
Previous Conclusion ◽  
Protein Coding Genes ◽  
Shared Function ◽  
High Gene

AbstractWe report the analysis of a 36-kbp region of the Neurospora crassa genome, which contains homologs of two closely linked stationary phase genes, SNZ1 and SNO1, from Saccharomyces cerevisiae. Homologs of SNZ1 encode extremely highly conserved proteins that have been implicated in pyridoxine (vitamin B6) metabolism in the filamentous fungi Cercospora nicotianae and in Aspergillus nidulans. In N. crassa, SNZ and SNO homologs map to the region occupied by pdx-1 (pyridoxine requiring), a gene that has been known for several decades, but which was not sequenced previously. In this study, pyridoxine-requiring mutants of N. crassa were found to possess mutations that disrupt conserved regions in either the SNZ or SNO homolog. Previously, nearly all of these mutants were classified as pdx-1. However, one mutant with a disrupted SNO homolog was at one time designated pdx-2. It now appears appropriate to reserve the pdx-1 designation for the N. crassa SNZ homolog and pdx-2 for the SNO homolog. We further report annotation of the entire 36,030-bp region, which contains at least 12 protein coding genes, supporting a previous conclusion of high gene densities (12,000-13,000 total genes) for N. crassa. Among genes in this region other than SNZ and SNO homologs, there was no evidence of shared function. Four of the genes in this region appear to have been lost from the S. cerevisiae lineage.

scholarly journals Mode of action and substrate specificities of cellulases from cloned bacterial genes.

1984 ◽  
Vol 259 (16) ◽  
pp. 10455-10459
Author(s):  
N R Gilkes ◽  
M L Langsford ◽  
D G Kilburn ◽  
R C Miller ◽  
R A Warren
Keyword(s):  
Mode Of Action ◽  
Substrate Specificities ◽  
Bacterial Genes

Induction and intracellular localization of the 80-kilodalton heat-shock protein of Neurospora crassa

1992 ◽  
Vol 70 (12) ◽  
pp. 1347-1355 ◽  
Author(s):  
H. S. Roychowdhury ◽  
T. J. MacAlister ◽  
J. W. Costerton ◽  
M. Kapoor
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Neurospora Crassa ◽  
Immunoelectron Microscopy ◽  
Intracellular Localization ◽  
Normal Growth ◽  
Immunogold Labelling ◽  
Subcellular Compartment ◽  
Intracellular Location ◽  
Gold Label

The most abundant heat-shock protein of Neurospora crassa is a multimeric glycoprotein of 80-kilodaltons (i.e., HSP80), induced strongly by hyperthermia and at a lower level by sodium arsenite, ethanol, and carbon source depletion. Immunoelectron microscopy, using indirect immunogold labelling demonstrated that HSP80 was undetectable in mycelium cultured at the normal growth temperature of 28 °C, but it appeared rapidly following the commencement of heat-shock treatment at 48 °C. HSP80, visualized by the gold label, was observed almost exclusively in the cytoplasm, exhibiting a uniform distribution. Association of this protein with cellular membranes and (or) targeting to a particular subcellular compartment or organelle was not apparent.Key words: 80-kilodalton heat-shock protein, Neurospora, intracellular location, immunoelectron microscopy.

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