Conservation of structure and function of the aflatoxin regulatory gene aflR from Aspergillus nidulans and A. flavus

SummarySex determination in Drosophila depends on the ratio of X chromosomes to sets of autosomes (X:A). This chromosomal signal is used to regulate a few control genes whose state of activity selects either the male or the female sexual pathway. We have studied the structure and function of dsx (double sex) which appears to be the last regulatory gene on whose function the sexual pathway eventually depends. We have mutagenized the locus, varied the doses of dominant dsx-mutations and wildtype alleles, and combined different dsx-alleles with recessive mutations in other sex-determining genes, such as ix, tra-2 and tra.The locus dsx harbours two genetic functions, dsxm to implement the male program, dsxf to implement the female program. We found that dsxm and dsxf can mutate independently although most mutations abolish both functions. We conclude that dsxm and dsxf each have their specific domain, but also share a large region of DNA that is essential for both functions. We present evidence that the dominant mutations correspond to a constitutive expression of the male-determining function dsxm, with the simultaneous abolishment of the female-determining function dsxf. This effect can be counteracted by two doses of expressed dsxf so that a female phenotype results. The products of one dose of expressed dsxm and one dose of expressed dsxf in the same cell appear to neutralize each other which leads to a null phenotype. The mutant combinations suggest that the product of dsxf requires the products of ix+, tra-2+ and tra+ to become functional.

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l-Arginine influences the structure and function of arginase mRNA in Aspergillus nidulans

Biological Chemistry ◽

10.1515/bc.2007.015 ◽

2007 ◽

Vol 388 (2) ◽

Cited By ~ 16

Author(s):

Piotr Borsuk ◽

Anna Przykorska ◽

Karina Blachnio ◽

Michal Koper ◽

Jerzy M. Pawlowicz ◽

...

Keyword(s):

Aspergillus Nidulans ◽

Structure And Function ◽

And Function

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Domain structure and function within the QUTA protein of Aspergillus nidulans: implications for the control of transcription

Microbiology ◽

10.1099/13500872-142-7-1909 ◽

1996 ◽

Vol 142 (7) ◽

pp. 1909-1909 ◽

Cited By ~ 1

Author(s):

I. Levesley ◽

G. H. Newton ◽

H. K. Lamb ◽

E. van Schothorst ◽

R. W. M. Dalgleish ◽

...

Keyword(s):

Aspergillus Nidulans ◽

Domain Structure ◽

Structure And Function ◽

And Function

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Structure and function of neural networks in the retina

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100102213 ◽

1988 ◽

Vol 46 ◽

pp. 26-27

Author(s):

Peter Sterling

Keyword(s):

Ganglion Cells ◽

Three Dimensional ◽

Structure And Function ◽

Synaptic Connections ◽

Visual Axis ◽

One Dimensional ◽

Cat Retina ◽

Ultrathin Sections ◽

And Function ◽

Insight Into

The synaptic connections in cat retina that link photoreceptors to ganglion cells have been analyzed quantitatively. Our approach has been to prepare serial, ultrathin sections and photograph en montage at low magnification (˜2000X) in the electron microscope. Six series, 100-300 sections long, have been prepared over the last decade. They derive from different cats but always from the same region of retina, about one degree from the center of the visual axis. The material has been analyzed by reconstructing adjacent neurons in each array and then identifying systematically the synaptic connections between arrays. Most reconstructions were done manually by tracing the outlines of processes in successive sections onto acetate sheets aligned on a cartoonist's jig. The tracings were then digitized, stacked by computer, and printed with the hidden lines removed. The results have provided rather than the usual one-dimensional account of pathways, a three-dimensional account of circuits. From this has emerged insight into the functional architecture.

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Osseointegration interface of calcified bone and endosseous implants

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100130110 ◽

1992 ◽

Vol 50 (2) ◽

pp. 1096-1097

Author(s):

K.E. Krizan ◽

J.E. Laffoon ◽

M.J. Buckley

Keyword(s):

Structure And Function ◽

Titanium Implants ◽

En Bloc ◽

Endosseous Implants ◽

Ultrastructural Studies ◽

The Past ◽

Cacodylate Buffer ◽

One Year ◽

And Function

With increase use of tissue-integrated prostheses in recent years it is a goal to understand what is happening at the interface between haversion bone and bulk metal. This study uses electron microscopy (EM) techniques to establish parameters for osseointegration (structure and function between bone and nonload-carrying implants) in an animal model. In the past the interface has been evaluated extensively with light microscopy methods. Today researchers are using the EM for ultrastructural studies of the bone tissue and implant responses to an in vivo environment. Under general anesthesia nine adult mongrel dogs received three Brånemark (Nobelpharma) 3.75 × 7 mm titanium implants surgical placed in their left zygomatic arch. After a one year healing period the animals were injected with a routine bone marker (oxytetracycline), euthanized and perfused via aortic cannulation with 3% glutaraldehyde in 0.1M cacodylate buffer pH 7.2. Implants were retrieved en bloc, harvest radiographs made (Fig. 1), and routinely embedded in plastic. Tissue and implants were cut into 300 micron thick wafers, longitudinally to the implant with an Isomet saw and diamond wafering blade [Beuhler] until the center of the implant was reached.

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Use of human autoantibodies and immunoelectron microscopy to study structure and function of the nucleolus and nuclear bodies

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100122939 ◽

1992 ◽

Vol 50 (1) ◽

pp. 506-507

Author(s):

Robert L. Ochs

Keyword(s):

Electron Microscopy ◽

Structure And Function ◽

Nuclear Bodies ◽

Nuclear Interior ◽

Coiled Bodies ◽

Interchromatin Granules ◽

And Function ◽

Conventional Electron Microscopy ◽

Perichromatin Granules ◽

Perichromatin Fibrils

By conventional electron microscopy, the formed elements of the nuclear interior include the nucleolus, chromatin, interchromatin granules, perichromatin granules, perichromatin fibrils, and various types of nuclear bodies (Figs. 1a-c). Of these structures, all have been reasonably well characterized structurally and functionally except for nuclear bodies. The most common types of nuclear bodies are simple nuclear bodies and coiled bodies (Figs. 1a,c). Since nuclear bodies are small in size (0.2-1.0 μm in diameter) and infrequent in number, they are often overlooked or simply not observed in any random thin section. The rat liver hepatocyte in Fig. 1b is a case in point. Historically, nuclear bodies are more prominent in hyperactive cells, they often occur in proximity to nucleoli (Fig. 1c), and sometimes they are observed to “bud off” from the nucleolar surface.

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Depletion and Reconstitution of Active E. Coli Ribosomes

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100116826 ◽

1975 ◽

Vol 33 ◽

pp. 640-641

Author(s):

M. Boublik ◽

W. Hellmann ◽

F. Jenkins

Keyword(s):

Protein Biosynthesis ◽

Large Subunit ◽

High Resolution Electron Microscopy ◽

Small Subunit ◽

Structure And Function ◽

Biologically Active ◽

Biological Macromolecules ◽

E Coli ◽

Resolution Electron ◽

And Function

Correlations between structure and function of biological macromolecules have been studied intensively for many years, mostly by indirect methods. High resolution electron microscopy is a unique tool which can provide such information directly by comparing the conformation of biopolymers in their biologically active and inactive state. We have correlated the structure and function of ribosomes, ribonucleoprotein particles which are the site of protein biosynthesis. 70S E. coli ribosomes, used in this experiment, are composed of two subunits - large (50S) and small (30S). The large subunit consists of 34 proteins and two different ribonucleic acid molecules. The small subunit contains 21 proteins and one RNA molecule. All proteins (with the exception of L7 and L12) are present in one copy per ribosome.This study deals with the changes in the fine structure of E. coli ribosomes depleted of proteins L7 and L12. These proteins are unique in many aspects.

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