A umuDC-independent SOS pathway for frameshift mutagenesis

1992 ◽  
Vol 235 (2-3) ◽  
pp. 373-380 ◽  
Author(s):  
G. Maenhaut-Michele ◽  
R. Janet-Bintz ◽  
R.P.P. Fuchs
2008 ◽  
Vol 471 (2) ◽  
pp. 146-158 ◽  
Author(s):  
Shilpi Mahajan ◽  
Girdhar K. Pandey ◽  
Narendra Tuteja

1981 ◽  
Vol 90 (1) ◽  
pp. 1-10 ◽  
Author(s):  
Peter R. Young ◽  
Rong-Ine Ma ◽  
Peter Marfey ◽  
Neville R. Kallenbach

Genetics ◽  
1983 ◽  
Vol 103 (3) ◽  
pp. 353-366
Author(s):  
Lynn S Ripley ◽  
Nadja B Shoemaker

ABSTRACT T4 DNA polymerase strongly influences the frequency and specificity of frameshift mutagenesis. Fifteen of 19 temperature-sensitive alleles of the DNA polymerase gene substantially influenced the reversion frequencies of frameshift mutations measured in the T4 rII genes. Most polymerase mutants increased frameshift frequencies, but a few alleles (previously noted as antimutators for base substitution mutations) decreased the frequencies of certain frameshifts while increasing the frequencies of others. The various patterns of enhanced or decreased frameshift mutation frequencies suggest that T4 DNA polymerase is likely to play a variety of roles in the metabolic events leading to frameshift mutation. A detailed genetic study of the specificity of the mutator properties of three DNA polymerase alleles (tsL56, tsL98 and tsL88) demonstrated that each produces a distinctive frameshift spectrum. Differences in frameshift frequencies at similar DNA sequences within the rII genes, the influence of mutant polymerase alleles on these frequencies, and the presence or absence of the dinucleotide sequence associated with initiation of Okazaki pieces at the frameshift site has led us to suggest that the discontinuities associated with discontinuous DNA replication may contribute to spontaneous frameshift mutation frequencies in T4.


2003 ◽  
Vol 279 (1) ◽  
pp. 207-215 ◽  
Author(s):  
Quan-Sheng Qiu ◽  
Yan Guo ◽  
Francisco J. Quintero ◽  
José M. Pardo ◽  
Karen S. Schumaker ◽  
...  

2007 ◽  
Vol 27 (22) ◽  
pp. 7781-7790 ◽  
Author(s):  
Giorgia Batelli ◽  
Paul E. Verslues ◽  
Fernanda Agius ◽  
Quansheng Qiu ◽  
Hiroaki Fujii ◽  
...  

ABSTRACT The salt overly sensitive (SOS) pathway is critical for plant salt stress tolerance and has a key role in regulating ion transport under salt stress. To further investigate salt tolerance factors regulated by the SOS pathway, we expressed an N-terminal fusion of the improved tandem affinity purification tag to SOS2 (NTAP-SOS2) in sos2-2 mutant plants. Expression of NTAP-SOS2 rescued the salt tolerance defect of sos2-2 plants, indicating that the fusion protein was functional in vivo. Tandem affinity purification of NTAP-SOS2-containing protein complexes and subsequent liquid chromatography-tandem mass spectrometry analysis indicated that subunits A, B, C, E, and G of the peripheral cytoplasmic domain of the vacuolar H+-ATPase (V-ATPase) were present in a SOS2-containing protein complex. Parallel purification of samples from control and salt-stressed NTAP-SOS2/sos2-2 plants demonstrated that each of these V-ATPase subunits was more abundant in NTAP-SOS2 complexes isolated from salt-stressed plants, suggesting that the interaction may be enhanced by salt stress. Yeast two-hybrid analysis showed that SOS2 interacted directly with V-ATPase regulatory subunits B1 and B2. The importance of the SOS2 interaction with the V-ATPase was shown at the cellular level by reduced H+ transport activity of tonoplast vesicles isolated from sos2-2 cells relative to vesicles from wild-type cells. In addition, seedlings of the det3 mutant, which has reduced V-ATPase activity, were found to be severely salt sensitive. Our results suggest that regulation of V-ATPase activity is an additional key function of SOS2 in coordinating changes in ion transport during salt stress and in promoting salt tolerance.


1984 ◽  
Vol 195 (3) ◽  
pp. 418-423 ◽  
Author(s):  
Thomas R. Skopek ◽  
Franklin Hutchinson

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