Characterization of a slow folding reaction for the α subunit of tryptophan synthase

1987 ◽  
Vol 2 (1) ◽  
pp. 54-63 ◽  
Author(s):  
Mark R. Hurle ◽  
Greg A. Michelotti ◽  
Mark M. Crisanti ◽  
C. Robert Matthews
Keyword(s):  
Tryptophan Synthase ◽  
Α Subunit

scholarly journals Characterization of the putative tryptophan synthase β-subunit from Mycobacterium tuberculosis

2009 ◽  
Vol 41 (5) ◽  
pp. 379-388 ◽  
Author(s):  
Hongbo Shen ◽  
Yanping Yang ◽  
Feifei Wang ◽  
Ying Zhang ◽  
Naihao Ye ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Tryptophan Synthase ◽  
Β Subunit

scholarly journals The G-Protein α-Subunit GasC Plays a Major Role in Germination in the Dimorphic FungusPenicillium marneffei

Genetics ◽  
2003 ◽  
Vol 164 (2) ◽  
pp. 487-499 ◽  
Author(s):  
Sophie Zuber ◽  
Michael J Hynes ◽  
Alex Andrianopoulos
Keyword(s):  
G Protein ◽  
Germination Rate ◽  
Yeast Cells ◽  
Class Iii ◽  
Temperature Dependent ◽  
Gene Encoding ◽  
Α Subunit ◽  
G Protein Α Subunit ◽  
Opportunistic Human Pathogen

AbstractThe opportunistic human pathogen Penicillium marneffei exhibits a temperature-dependent dimorphic switch. At 25°, multinucleate, septate hyphae that can undergo differentiation to produce asexual spores (conidia) are produced. At 37° hyphae undergo arthroconidiation to produce uninucleate yeast cells that divide by fission. This work describes the cloning of the P. marneffei gasC gene encoding a G-protein α-subunit that shows high homology to members of the class III fungal Gα-subunits. Characterization of a ΔgasC mutant and strains carrying a dominant-activating gasCG45R or a dominant-interfering gasCG207R allele show that GasC is a crucial regulator of germination. A ΔgasC mutant is severely delayed in germination, whereas strains carrying a dominant-activating gasCG45R allele show a significantly accelerated germination rate. Additionally, GasC signaling positively affects the production of the red pigment by P. marneffei at 25° and negatively affects the onset of conidiation and the conidial yield, showing that GasC function overlaps with functions of the previously described Gα-subunit GasA. In contrast to the S. cerevisiae ortholog Gpa2, our data indicate that GasC is not involved in carbon or nitrogen source sensing and plays no major role in either hyphal or yeast growth or in the switch between these two forms.

Discovery and characterization of a novel splice variant of the GM-CSF receptor α subunit

2007 ◽  
Vol 35 (10) ◽  
pp. 1483-1494 ◽  
Author(s):  
Jennifer L. Pelley ◽  
Chris D. Nicholls ◽  
Tara L. Beattie ◽  
Christopher B. Brown
Keyword(s):  
Splice Variant ◽  
Α Subunit ◽  
Gm Csf

scholarly journals Baculovirus expression of two protein disulphide isomerase isoforms from Caenorhabditis elegans and characterization of prolyl 4-hydroxylases containing one of these polypeptides as their β subunit

1996 ◽  
Vol 317 (3) ◽  
pp. 721-729 ◽  
Author(s):  
Johanna VEIJOLA ◽  
Pia ANNUNEN ◽  
Peppi KOIVUNEN ◽  
Antony P. PAGE ◽  
Taina PIHLAJANIEMI ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Cloning And Expression ◽  
Β Subunit ◽  
Α Subunit ◽  
Protein Disulphide Isomerase ◽  
C Elegans ◽  
Baculovirus Expression ◽  
Expression Studies ◽  
Α Subunits

Protein disulphide isomerase (PDI; EC 5.3.4.1) is a multifunctional polypeptide that is identical to the β subunit of prolyl 4-hydroxylases. We report here on the cloning and expression of the Caenorhabditis elegans PDI/β polypeptide and its isoform. The overall amino acid sequence identity and similarity between the processed human and C. elegans PDI/β polypeptides are 61% and 85% respectively, and those between the C. elegans PDI/β polypeptide and the PDI isoform 46% and 73%. The isoform differs from the PDI/β and ERp60 polypeptides in that its N-terminal thioredoxin-like domain has an unusual catalytic site sequence -CVHC-. Expression studies in insect cells demonstrated that the C. elegans PDI/β polypeptide forms an active prolyl 4-hydroxylase α2β2 tetramer with the human α subunit and an αβ dimer with the C. elegans α subunit, whereas the C. elegans PDI isoform formed no prolyl 4-hydroxylase with either α subunit. Removal of the 32-residue C-terminal extension from the C. elegans α subunit totally eliminated αβ dimer formation. The C. elegans PDI/β polypeptide formed less prolyl 4-hydroxylase with both the human and C. elegans α subunits than did the human PDI/β polypeptide, being particularly ineffective with the C. elegans α subunit. Experiments with hybrid polypeptides in which the C-terminal regions had been exchanged between the human and C. elegans PDI/β polypeptides indicated that differences in the C-terminal region are one reason, but not the only one, for the differences in prolyl 4-hydroxylase formation between the human and C. elegans PDI/β polypeptides. The catalytic properties of the C. elegans prolyl 4-hydroxylase αβ dimer were very similar to those of the vertebrate type II prolyl 4-hydroxylase tetramer, including the Km for the hydroxylation of long polypeptide substrates.

scholarly journals Entropic Stabilization of the Tryptophan Synthase α-Subunit from a Hyperthermophile,Pyrococcus furiosus

2000 ◽  
Vol 276 (14) ◽  
pp. 11062-11071 ◽  
Author(s):  
Yuriko Yamagata ◽  
Kyoko Ogasahara ◽  
Yusaku Hioki ◽  
Soo Jae Lee ◽  
Atsushi Nakagawa ◽  
...  
Keyword(s):  
Pyrococcus Furiosus ◽  
Tryptophan Synthase ◽  
Α Subunit ◽  
Entropic Stabilization
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