scholarly journals A Second PDZ-Containing Serine Protease Contributes to Activation of the Sporulation Transcription Factor σK in Bacillus subtilis

2003 ◽  
Vol 185 (20) ◽  
pp. 6051-6056 ◽  
Author(s):  
Qi Pan ◽  
Richard Losick ◽  
David Z. Rudner
Keyword(s):  
Transcription Factor ◽  
Bacillus Subtilis ◽  
Serine Protease ◽  
Signal Transduction Pathway ◽  
Transduction Pathway ◽  
Protein Protein Interaction ◽  
Interaction Domains ◽  
Carboxyl Terminal ◽  
Processing Protease ◽  
Fine Tune

ABSTRACT Gene expression late during the process of sporulation in Bacillus subtilis is governed by a multistep, signal transduction pathway involving the transcription factor σK, which is derived by regulated proteolysis from the inactive proprotein pro-σK. Processing of pro-σK is triggered by a signaling protein known as SpoIVB, a serine protease that contains a region with similarity to the PDZ family of protein-protein interaction domains. Here we report the discovery of a second PDZ-containing serine protease called CtpB that contributes to the activation of the pro-σK processing pathway. CtpB is a sporulation-specific, carboxyl-terminal processing protease and shares several features with SpoIVB. We propose that CtpB acts to fine-tune the regulation of pro-σK processing, and we discuss possible models by which CtpB influences the σK activation pathway.

Transcription factor ATF2 regulation by the JNK signal transduction pathway

Science ◽  
1995 ◽  
Vol 267 (5196) ◽  
pp. 389-393 ◽  
Author(s):  
S. Gupta ◽  
D. Campbell ◽  
B. Derijard ◽  
R. Davis
Keyword(s):  
Signal Transduction ◽  
Transcription Factor ◽  
Signal Transduction Pathway ◽  
Transduction Pathway

scholarly journals Protein-Protein Interaction Affinity Plays a Crucial Role in Controlling the Sho1p-Mediated Signal Transduction Pathway in Yeast

2004 ◽  
Vol 14 (6) ◽  
pp. 813-823 ◽  
Author(s):  
Jennifer A Marles ◽  
Samira Dahesh ◽  
Jennifer Haynes ◽  
Brenda J Andrews ◽  
Alan R Davidson
Keyword(s):  
Signal Transduction ◽  
Protein Interaction ◽  
Crucial Role ◽  
Signal Transduction Pathway ◽  
Transduction Pathway ◽  
Protein Protein Interaction

scholarly journals Genetic evidence for signal transduction within the Bacillus subtilis GerA germinant receptor

2021 ◽  
Author(s):  
Jeremy D. Amon ◽  
Lior Artzi ◽  
David Z. Rudner
Keyword(s):  
Signal Transduction ◽  
Bacillus Subtilis ◽  
Signal Transduction Pathway ◽  
Dominant Negative ◽  
Transduction Pathway ◽  
Sense And Respond ◽  
Enrichment Strategy ◽  
Functional Receptor

Bacterial spores can rapidly exit dormancy through the process of germination. This process begins with the activation of nutrient receptors embedded in the spore membrane. The prototypical germinant receptor in Bacillus subtilis responds to L-alanine and is thought to be a complex of proteins encoded by the genes in the gerA operon: gerAA , gerAB , and gerAC . The GerAB subunit has recently been shown to function as the nutrient sensor, but beyond contributing to complex stability, no additional functions have been attributed to the other two subunits. Here, we investigate the role of GerAA. We resurrect a previously characterized allele of gerA (termed gerA* ) that carries a mutation in gerAA and show it constitutively activates germination even in the presence of a wild-type copy of gerA . Using an enrichment strategy to screen for suppressors of gerA* , we identified mutations in all three gerA genes that restore a functional receptor. Characterization of two distinct gerAB suppressors revealed that one ( gerAB[E105K]) reduces the GerA complex's ability to respond to L-alanine, while another ( gerAB[F259S] ) disrupts the germinant signal downstream of L-alanine recognition. These data argue against models in which GerAA is directly or indirectly involved in germinant sensing. Rather, our data suggest that GerAA is responsible for transducing the nutrient signal sensed by GerAB. While the steps downstream of gerAA have yet to be uncovered, these results validate the use of a dominant-negative genetic approach in elucidating the gerA signal transduction pathway. Importance Endospore formers are a broad group of bacteria that can enter dormancy upon starvation and exit dormancy upon sensing the return of nutrients. How dormant spores sense and respond to these nutrients is poorly understood. Here, we identify a key step in the signal transduction pathway that is activated after spores detect the amino acid L-alanine. We present a model that provides a more complete picture of this process that is critical for allowing dormant spores to germinate and resume growth.

scholarly journals A SNP Mutation of SiCRC Regulates Seed Number Per Capsule and Capsule Length of cs1 Mutant in Sesame

2019 ◽  
Vol 20 (16) ◽  
pp. 4056
Author(s):  
Libin Wei ◽  
Chun Li ◽  
Yinghui Duan ◽  
Wenwen Qu ◽  
Huili Wang ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Transcription Factor ◽  
Signal Transduction Pathway ◽  
Gene Interaction ◽  
Transduction Pathway ◽  
Seed Number ◽  
Mechanism Study ◽  
Mutant Type ◽  
Genome Screening ◽  
Auxin Signal Transduction

Seed number per capsule (SNC) is a major factor influencing seed yield and is an important trait with complex gene interaction effects. We first performed genetic analysis, gene cloning, and molecular mechanism study for an EMS-induced sesame mutant cs1 with fewer SNC and shorter capsule length (CL). The mutant traits were due to the pleiotropism of a regressive gene (Sics1). Capsule hormone determination showed that five out of 12 hormones, including auxin indole-3-acetic acid (IAA), had significantly different levels between wild type (WT) and mutant type (MT). KEGG pathway analysis showed that plant hormone signal transduction, especially the auxin signal transduction pathway, was the most abundant differentially expressed signaling pathway. After the cross-population association and regional genome screening, we found that three homozygous loci were retained in cs1. Further analysis of these three loci resulted in the identification of SiCRC as the candidate gene for cs1. SiCRC consists of seven exons and six introns encoding 163 amino acids. The SiCRC in cs1 showed a point mutation at intron 5 and exon 6 junction, resulting in the splice site being frame-shifted eight nucleotides further downstream, causing incorrect splicing. Taken together, we assumed the SNP mutation in SiCRC disrupted the function of the transcription factor, which might act downstream of the CRC-auxin signal transduction pathway, resulting in a shorter CL and less SNC mutation of cs1 in sesame. Our results highlight the molecular framework underlying the transcription factor CRC-mediated role of auxin transduction in SNC and CL development.

scholarly journals Modulation of β-Catenin Phosphorylation/Degradation by Cyclin-dependent Kinase 2

2004 ◽  
Vol 279 (19) ◽  
pp. 19592-19599 ◽  
Author(s):  
Chun Shik Park ◽  
Sung Il Kim ◽  
Mi Su Lee ◽  
Cho-ya Youn ◽  
Dae Joong Kim ◽  
...  
Keyword(s):  
Cyclin E ◽  
Signal Transduction Pathway ◽  
Transduction Pathway ◽  
Cyclin Dependent Kinase ◽  
Rapid Degradation ◽  
Subsequent Degradation ◽  
Proteasome Pathway ◽  
Fine Tune

β-Catenin functions as a downstream component of the Wnt/Wingless signal transduction pathway, and inappropriate control of cytosolic β-catenin is a crucial step in the genesis of several human cancers. Here we demonstrate that cyclin-dependent kinase 2 (CDK2) in association with cyclin A or cyclin E directly binds to β-catenin.In vivoandin vitrokinase assays with cyclin-CDK2 demonstrate β-catenin phosphorylation on residues Ser33, Ser37, Thr41, and Ser45. This phosphorylation promotes rapid degradation of cytosolic β-catenin via the β-TrCP-mediated proteasome pathway. Moreover, cyclin E-CDK2 contributes to rapid degradation of cytosolic β-catenin levels during G1phase by regulating β-catenin phosphorylation and subsequent degradation. In this way, CDK2 may “fine tune” β-catenin levels over the course of the cell cycle.

scholarly journals Activation of the Proprotein Transcription Factor Pro-ςE Is Associated with Its Progression through Three Patterns of Subcellular Localization during Sporulation in Bacillus subtilis

1998 ◽  
Vol 180 (9) ◽  
pp. 2426-2433 ◽  
Author(s):  
Antje Hofmeister
Keyword(s):  
Transcription Factor ◽  
Bacillus Subtilis ◽  
Subcellular Localization ◽  
Cytoplasmic Membrane ◽  
Immunofluorescence Microscopy ◽  
Active Form ◽  
Signal Transduction Pathway ◽  
Subcellular Fractionation ◽  
Membrane Association ◽  
Chemical Cross Linking

ABSTRACT The activity of the sporulation transcription factor ςE in Bacillus subtilis is governed by an intercellular signal transduction pathway that controls the conversion of the inactive proprotein pro-ςE to the mature and active form of the factor. Here I use immunofluorescence microscopy to show that the activation of the proprotein is associated with its progression through three patterns of subcellular localization. In the predivisional sporangium, pro-ςE was found to be associated with the cytoplasmic membrane. Next, at the stage of asymmetric division, pro-ςE accumulated at the sporulation septum. Finally, after processing, mature ςEwas found to be distributed throughout the mother cell cytoplasm. The results of subcellular fractionation and sedimentation in density gradients of extracts prepared from postdivisional sporangia confirmed that pro-ςE was chiefly present in the membrane fraction and that ςE was predominantly cytoplasmic, findings that suggest that the pro-amino acid sequence is responsible for the sequestration of pro-ςE to the membrane. The results of chemical cross-linking experiments showed that pro-ςE was present in a complex with its putative processing protein, SpoIIGA, or with a protein that depended on SpoIIGA. The membrane association of pro-ςE was, however, independent of SpoIIGA and other proteins specific to B. subtilis. Likewise, accumulation of pro-ςE at the septum did not depend on its interaction with SpoIIGA. Sequestration of pro-ςE to the membrane might serve to facilitate its interaction with SpoIIGA and may be important for preventing its premature association with core RNA polymerase. The implications of these findings for the compartmentalization of ςE are discussed.

scholarly journals A protein-protein interaction map of the TNF-induced NF-κB signal transduction pathway

2018 ◽  
Vol 5 (1) ◽  
Author(s):  
Emmy Van Quickelberghe ◽  
Delphine De Sutter ◽  
Geert van Loo ◽  
Sven Eyckerman ◽  
Kris Gevaert
Keyword(s):  
Signal Transduction ◽  
Protein Interaction ◽  
Signal Transduction Pathway ◽  
Transduction Pathway ◽  
Protein Protein Interaction ◽  
Interaction Map
Sign in / Sign up

Export Citation Format

Share Document