scholarly journals Structural gene for the alkaline extracellular protease of Saccharomycopsis lipolytica.

1981 ◽  
Vol 145 (1) ◽  
pp. 404-409 ◽  
Author(s):  
P C Simms ◽  
D M Ogrydziak
Keyword(s):  
Structural Gene ◽  
Extracellular Protease ◽  
Saccharomycopsis Lipolytica

Alkaline Extracellular Protease Produced by Saccharomycopsis lipolytica CX161-1B

Microbiology ◽  
1982 ◽  
Vol 128 (6) ◽  
pp. 1225-1234 ◽  
Author(s):  
D. M. Ogrydziak ◽  
S. J. Scharf
Keyword(s):  
Extracellular Protease ◽  
Saccharomycopsis Lipolytica

scholarly journals GENETICS OF EXTRACELLULAR PROTEASE PRODUCTION IN SACCHAROMYCOPSIS LIPOLYTICA

Genetics ◽  
1977 ◽  
Vol 87 (4) ◽  
pp. 621-632
Author(s):  
David M Ogrydziak ◽  
Robert K Mortimer
Keyword(s):  
Extracellular Enzymes ◽  
Skim Milk ◽  
Extracellular Enzyme ◽  
Extracellular Protease ◽  
Protease Production ◽  
Mating Frequency ◽  
Wild Type ◽  
Saccharomycopsis Lipolytica ◽  
Complementation Groups ◽  
Membrane Components

ABSTRACT Mutants of Saccharomycopsis lipolytica with reduced ability to produce zones of clearing on skim-milk agar plates were isolated and their properties studied. For 18 mutants it was possible to score unambiguously segregants of crosses between these mutants and wild type for extracellular protease production. These mutants all produce reduced levels of extracellular protease in liquid culture. The mutations are recessive and are in nuclear genes. The 18 mutations define 10 or 11 complementation groups, no two of which are closely linked. Mutants in four of the complementation groups also produced reduced levels of extracellular RNAse, and the reduced levels of extracellular protease and RNAse production segregate together. Five of the mutants exhibited reduced mating frequency, and one mutant was osmotic remedial for extracellular protease production. These results demonstrate that many genes can affect extracellular protease production. Besides mutations in the structural gene and in regulatory genes, mutations are likely to be in genes involved in steps common to the production of several extracellular enzymes or in genes coding for cell wall or membrane components necessary for extracellular enzyme production.

scholarly journals Characterization of Saccharomycopsis lipolytica Mutants Producing Lowered Levels of Alkaline Extracellular Protease

Microbiology ◽  
1982 ◽  
Vol 128 (10) ◽  
pp. 2271-2280 ◽  
Author(s):  
D. M. Ogrydziak ◽  
S.-C. Cheng ◽  
S. J. Scharf
Keyword(s):  
Extracellular Protease ◽  
Saccharomycopsis Lipolytica

Bt1, a structural gene for the major 39-44 kDa amyloplast membrane polypeptides

1995 ◽  
Vol 95 (2) ◽  
pp. 176-186 ◽  
Author(s):  
Heping Cao ◽  
Thomas D. Sullivan ◽  
Charles D. Boyer ◽  
Jack C. Shannon
Keyword(s):  
Structural Gene

Optimization of growth conditions and production of extracellular protease by Bacillus subtilis DC5

2015 ◽  
Vol 37 (1se) ◽  
Author(s):  
Do Thi Bich Thuy ◽  
Phan Thi Be ◽  
Doan Thi Thanh Thao
Keyword(s):  
Bacillus Subtilis ◽  
Growth Conditions ◽  
Extracellular Protease

scholarly journals A NEW MAP LOCATION FOR THE ilvB LOCUS OF ESCHERICHIA COLI

Genetics ◽  
1980 ◽  
Vol 96 (1) ◽  
pp. 59-77
Author(s):  
Thomas C Newman ◽  
Mark Levinthal
Keyword(s):  
Escherichia Coli ◽  
Structural Gene ◽  
Acetolactate Synthase ◽  
Deletion Mapping ◽  
Donor Strain ◽  
E Coli ◽  
Linkage Of Genes ◽  
Map Location ◽  
New Alleles

ABSTRACT We isolated, in E. coli K12, new alleles of the ilvB locus, the structural gene for acetolactate synthase isoenzyme I, and showed them to map at or near the ilvB619 site. The map position of the ilvB locus was redetermined because plasmids containing the ilvC-cya portion of the chromosome did not complement mutations at the ilvB locus. Furthermore, diploids for the ilvEDAC genes formed with these plasmids in an ilvHI background facilitated the isolation of the new ilvB alleles. The ilvB locus was remapped and found to be located at 81.5 minutes, between the uhp and dnaA loci. This location was determined by two- and three-point transductional crosses, deletion mapping and complementation with newly isolated plasmids. One of the new alleles of the ilvB gene is a mu-1 insertion. When present in the donor strain, this allele interferes with the linkage of genes flanking the mu-1 insertion, as well as the linkage of genes to either side of the mu-1 insertion.

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