scholarly journals A third envelope stress signal transduction pathway in Escherichia coli

2002 ◽  
Vol 45 (6) ◽  
pp. 1599-1611 ◽  
Author(s):  
Robert G. Raffa ◽  
Tracy L. Raivio
1994 ◽  
Vol 5 (3) ◽  
pp. 297-312 ◽  
Author(s):  
J A Brill ◽  
E A Elion ◽  
G R Fink

We have isolated dominant gain-of-function (gf) mutations in FUS3, a Saccharomyces cerevisiae mitogen-activated protein (MAP) kinase homolog, that constitutively activate the yeast mating signal transduction pathway and confer hypersensitivity to mating pheromone. Surprisingly, the phenotypes of dominant FUS3gf mutations require the two protein kinases, STE7 and STE11. FUS3gf kinases are hyperphosphorylated in yeast independently of STE7. Consistent with this, FUS3gf kinases expressed in Escherichia coli exhibit an increased ability to autophosphorylate on tyrosine in vivo. FUS3gf mutations suppress the signal transduction defect of a severely catalytically impaired allele of STE7. This finding suggests that the tyrosine-phosphorylated form of FUS3 is a better substrate for activation by STE7. Furthermore, these results imply that the degree of autophosphorylation of a MAP kinase determines its threshold of sensitivity to upstream signals.


2004 ◽  
Vol 186 (13) ◽  
pp. 4326-4337 ◽  
Author(s):  
Yvonne M. Lee ◽  
Patricia A. DiGiuseppe ◽  
Thomas J. Silhavy ◽  
Scott J. Hultgren

ABSTRACT P pilus biogenesis occurs via the highly conserved chaperone-usher pathway, and assembly is monitored by the CpxRA two-component signal transduction pathway. Structural pilus subunits consist of an N-terminal extension followed by an incomplete immunoglobulin-like fold that is missing a C-terminal seventh beta strand. In the pilus fiber, the immunoglobulin-like fold of each pilin is completed by the N-terminal extension of its neighbor. Subunits that do not get incorporated into the pilus fiber are driven “OFF-pathway.” In this study, we found that PapE was the only OFF-pathway nonadhesin P pilus subunit capable of activating Cpx. Manipulation of the PapE structure by removing, relocating within the protein, or swapping its N-terminal extension with that of other subunits altered the protein's self-associative and Cpx-activating properties. The self-association properties of the new subunits were dictated by the specific N-terminal extension provided and were consistent with the order of the subunits in the pilus fiber. However, these aggregation properties did not directly correlate with Cpx induction. Cpx activation instead correlated with the presence or absence of an N-terminal extension in the PapE pilin structure. Removal of the N-terminal extension of PapE was sufficient to abolish Cpx activation. Replacement of an N-terminal extension at either the amino or carboxyl terminus restored Cpx induction. Thus, the data presented in this study argue that PapE has features inherent in its structure or during its folding that act as specific inducers of Cpx signal transduction.


2020 ◽  
Vol 7 (1) ◽  
Author(s):  
Keqin Chen ◽  
Yunna Guo ◽  
Mengru Song ◽  
Lifu Liu ◽  
Hao Xue ◽  
...  

AbstractClarifying the stress signal transduction pathway would be helpful for understanding the abiotic stress resistance mechanism in apple (Malus × domestica Borkh.) and could assist in the development of new varieties with high stress tolerance by genetic engineering. The key NAC transcription factor SND1, which is involved in the lignin biosynthesis process in apple, was functionally analyzed. The results of the stress treatments indicated that MdSND1 could be induced by salt, mannitol and ABA. Compared with wild-type GL-3 plants, MdSND1-overexpressing apple plants with greater antioxidant capacity and lignin were more resistant to salt and simulated osmotic stress, while RNAi plants were more vulnerable. Additionally, molecular experiments confirmed that MdSND1 could regulate the biosynthesis of lignin by activating the transcription of MdMYB46/83. Moreover, genes known to be involved in the stress signal transduction pathway (MdAREB1A, MdAREB1B, MdDREB2A, MdRD29A, and MdRD22) were screened for their close correlations with the expression of MdSND1 and the response to salt and osmotic stress. Multiple verification tests further demonstrated that MdSND1 could directly bind to these gene promoters and activate their transcription. The above results revealed that MdSND1 is directly involved in the regulation of lignin biosynthesis and the signal transduction pathway involved in the response to both salt and osmotic stress in apple.


2004 ◽  
Vol 135 (3) ◽  
pp. 1685-1696 ◽  
Author(s):  
Orna Avsian-Kretchmer ◽  
Yardena Gueta-Dahan ◽  
Simcha Lev-Yadun ◽  
Rachel Gollop ◽  
Gozal Ben-Hayyim

2001 ◽  
Vol 183 (19) ◽  
pp. 5768-5771 ◽  
Author(s):  
Sally M. Hoffer ◽  
Jan Tommassen

ABSTRACT Disruption of pstS encoding the Pi-binding protein in Escherichia coli generally leads to the constitutive expression of thepho regulon. We demonstrate that Pi-controlled expression is restored when the activity of the Pitransporter PitA or PitB is increased. Apparently, PstS is not an essential component of the signal transduction pathway.


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