Analysis of a temperature sensitive mutation in gene cII of bacteriophage lambda

1976 ◽  
Vol 149 (1) ◽  
pp. 121-123 ◽  
Author(s):  
Amos B. Oppenheim ◽  
Irit Kapeller
1990 ◽  
Vol 10 (5) ◽  
pp. 1908-1914
Author(s):  
C Martin ◽  
S Okamura ◽  
R Young

The two large subunits of RNA polymerase II, RPB1 and RPB2, contain regions of extensive homology to the two large subunits of Escherichia coli RNA polymerase. These homologous regions may represent separate protein domains with unique functions. We investigated whether suppressor genetics could provide evidence for interactions between specific segments of RPB1 and RPB2 in Saccharomyces cerevisiae. A plasmid shuffle method was used to screen thoroughly for mutations in RPB2 that suppress a temperature-sensitive mutation, rpb1-1, which is located in region H of RPB1. All six RPB2 mutations that suppress rpb1-1 were clustered in region I of RPB2. The location of these mutations and the observation that they were allele specific for suppression of rpb1-1 suggests an interaction between region H of RPB1 and region I of RPB2. A similar experiment was done to isolate and map mutations in RPB1 that suppress a temperature-sensitive mutation, rpb2-2, which occurs in region I of RPB2. These suppressor mutations were not clustered in a particular region. Thus, fine structure suppressor genetics can provide evidence for interactions between specific segments of two proteins, but the results of this type of analysis can depend on the conditional mutation to be suppressed.


Yeast ◽  
2008 ◽  
Vol 25 (3) ◽  
pp. 219-233 ◽  
Author(s):  
Xunying Shan ◽  
Tara A. Russell ◽  
Scott M. Paul ◽  
David B. Kushner ◽  
Paul B. M. Joyce

Development ◽  
1978 ◽  
Vol 47 (1) ◽  
pp. 111-120
Author(s):  
M. Bownes ◽  
B. D. Hames

A number of female sterile mutations on the first and third chromosomes of Drosophila melanogaster have been screened for defects in the yolk proteins using polyacrylamide gel electrophoresis. Two new mutants were identified. 6m45 accumulates all three yolk proteins (YP1, YP2 and YP3) in the haemolymph but they are all absent from the ovaries suggesting it is a yolk-protein-uptake mutant. In contrast, 1163 is a temperature-sensitive mutation with a large reduction in the quantity of YP1 in the haemolymph and ovaries at 29 °C. Both mutants are autonomous in ovary transplant experiments.


2002 ◽  
Vol 13 (5) ◽  
pp. 1594-1607 ◽  
Author(s):  
Sangiliyandi Gurunathan ◽  
Michael Marash ◽  
Adina Weinberger ◽  
Jeffrey E. Gerst

Earlier we demonstrated that activation of a ceramide-activated protein phosphatase (CAPP) conferred normal growth and secretion to yeast lacking their complement of exocytic v-SNAREs (Snc1,2) or bearing a temperature-sensitive mutation in an exocytic t-SNARE (Sso2). CAPP activation led to Sso dephosphorylation and enhanced the assembly of t-SNAREs into functional complexes. Thus, exocytosis in yeast is modulated by t-SNARE phosphorylation. Here, we show that endocytic defects in cells lacking the v- and t-SNAREs involved in endocytosis are also rescued by CAPP activation. Yeast lacking the Tlg1 or Tlg2 t-SNAREs, the Snc v-SNAREs, or both, undergo endocytosis after phosphatase activation. CAPP activation correlated with restored uptake of FM4-64 to the vacuole, the uptake and degradation of the Ste2 receptor after mating factor treatment, and the dephosphorylation and assembly of Tlg1,2 into SNARE complexes. Activation of the phosphatase by treatment with C2-ceramide,VBM/ELO gene inactivation, or by the overexpression of SIT4 was sufficient to confer rescue. Finally, we found that mutation of single PKA sites in Tlg1 (Ser31 to Ala31) or Tlg2 (Ser90 to Ala90) was sufficient to restore endocytosis, but not exocytosis, to snc cells. These results suggest that endocytosis is also modulated by t-SNARE phosphorylation in vivo.


2000 ◽  
Vol 276 (12) ◽  
pp. 9308-9315 ◽  
Author(s):  
Debasish Sinha ◽  
M. Keith Wyatt ◽  
Robert Sarra ◽  
Cynthia Jaworski ◽  
Christine Slingsby ◽  
...  

2000 ◽  
Vol 182 (10) ◽  
pp. 2989-2991 ◽  
Author(s):  
Katherine P. Lemon ◽  
Iren Kurtser ◽  
Judy Wu ◽  
Alan D. Grossman

ABSTRACT Initiation of spore formation in Bacillus subtilisappears to depend on initiation of DNA replication. This regulation was first identified using a temperature-sensitive mutation indnaB. We found that mutations in the replication initiation genes dnaA and dnaD also inhibit sporulation, indicating that inhibition of sporulation is triggered by general defects in the function of replication initiation proteins.


Virology ◽  
1980 ◽  
Vol 101 (1) ◽  
pp. 281-285 ◽  
Author(s):  
Daniel Schümperli ◽  
Grant McFadden ◽  
R. Wyler ◽  
Samuel Dales

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