An active proteolytic derivative of the .alpha. subunit of tryptophan synthase. Identification of the site of cleavage and characterization of the fragments

Biochemistry ◽  
1979 ◽  
Vol 18 (22) ◽  
pp. 4827-4835 ◽  
Author(s):  
William Higgins ◽  
Thomas Fairwell ◽  
Edith Wilson Miles
Keyword(s):  
Alpha Subunit ◽  
Tryptophan Synthase

Characterization of tryptophan synthase alpha subunit mutants of Arabidopsis thaliana

1996 ◽  
Vol 253 (3) ◽  
pp. 353-361 ◽  
Author(s):  
E. R. Radwanski ◽  
A. J. Barczak ◽  
R. L. Last
Keyword(s):  
Arabidopsis Thaliana ◽  
Alpha Subunit ◽  
Tryptophan Synthase

Characterization of tryptophan synthase alpha subunit mutants of

1996 ◽  
Vol 253 (3) ◽  
pp. 353 ◽  
Author(s):  
E. R. Radwanski ◽  
A. J. Barczak ◽  
R. L. Last
Keyword(s):  
Alpha Subunit ◽  
Tryptophan Synthase

scholarly journals 5-Fluoroindole resistance identifies tryptophan synthase beta subunit mutants in Arabidopsis thaliana.

Genetics ◽  
1995 ◽  
Vol 140 (1) ◽  
pp. 303-313
Author(s):  
A J Barczak ◽  
J Zhao ◽  
K D Pruitt ◽  
R L Last
Keyword(s):  
Arabidopsis Thaliana ◽  
Protein A ◽  
Beta Subunit ◽  
Alpha Subunit ◽  
Anthranilate Synthase ◽  
Tryptophan Synthase ◽  
Wild Type ◽  
Recessive Mutations ◽  
The Stability

Abstract A study of the biochemical genetics of the Arabidopsis thaliana tryptophan synthase beta subunit was initiated by characterization of mutants resistant to the inhibitor 5-fluoroindole. Thirteen recessive mutations were recovered that are allelic to trp2-1, a mutation in the more highly expressed of duplicate tryptophan synthase beta subunit genes (TSB1). Ten of these mutations (trp2-2 through trp2-11) cause a tryptophan requirement (auxotrophs), whereas three (trp2-100 through trp2-102) remain tryptophan prototrophs. The mutations cause a variety of changes in tryptophan synthase beta expression. For example, two mutations (trp2-5 and trp2-8) cause dramatically reduced accumulation of TSB mRNA and immunologically detectable protein, whereas trp2-10 is associated with increased mRNA and protein. A correlation exists between the quantity of mutant beta and wild-type alpha subunit levels in the trp2 mutant plants, suggesting that the synthesis of these proteins is coordinated or that the quantity or structure of the beta subunit influences the stability of the alpha protein. The level of immunologically detectable anthranilate synthase alpha subunit protein is increased in the trp2 mutants, suggesting the possibility of regulation of anthranilate synthase levels in response to tryptophan limitation.

Characterization of the slow steps in the folding of the .alpha. subunit of tryptophan synthase

Biochemistry ◽  
1981 ◽  
Vol 20 (9) ◽  
pp. 2700-2706 ◽  
Author(s):  
Mark M. Crisanti ◽  
C. Robert Matthews
Keyword(s):  
Alpha Subunit ◽  
Tryptophan Synthase

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
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