Heme: emergent roles of heme in signal transduction, functional regulation and as catalytic centres

2019 ◽  
Vol 48 (24) ◽  
pp. 5624-5657 ◽  
Author(s):  
Toru Shimizu ◽  
Alzbeta Lengalova ◽  
Václav Martínek ◽  
Markéta Martínková
Keyword(s):  
Signal Transduction ◽  
Protein Kinase ◽  
Dna Binding ◽  
Heme Proteins ◽  
Molecular Mechanisms ◽  
Kinase Activity ◽  
Bond Formation ◽  
Dna Binding Protein ◽  
Protein Kinase Activity ◽  
Functional Regulation

Molecular mechanisms of unprecedented functions of exchangeable/labile heme and heme proteins including transcription, DNA binding, protein kinase activity, K+ channel functions, cis–trans isomerization, N–N bond formation, and other functions are described.

scholarly journals High salt- and SDS-stable DNA binding protein complexes with ATPase and protein kinase activity retained in chromatin-depleted nuclei

1995 ◽  
Vol 23 (8) ◽  
pp. 1359-1366 ◽  
Author(s):  
Benediktas Juodka ◽  
Eberhard Spiess ◽  
Antonella Angiolillo ◽  
Gaby Joswig ◽  
Karsten Rothbarth ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Dna Binding ◽  
Kinase Activity ◽  
Protein Complexes ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
High Salt ◽  
Protein Kinase Activity

scholarly journals Characterization of a Ku86 Variant Protein That Results in Altered DNA Binding and Diminished DNA-dependent Protein Kinase Activity

1996 ◽  
Vol 271 (24) ◽  
pp. 14098-14104 ◽  
Author(s):  
Zhiyong Han ◽  
Christine Johnston ◽  
Westley H. Reeves ◽  
Timothy Carter ◽  
James H. Wyche ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Dna Binding ◽  
Kinase Activity ◽  
Protein Kinase Activity ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
Variant Protein

scholarly journals Yeast Mpk1 Mitogen-Activated Protein Kinase Activates Transcription through Swi4/Swi6 by a Noncatalytic Mechanism That Requires Upstream Signal

2008 ◽  
Vol 28 (8) ◽  
pp. 2579-2589 ◽  
Author(s):  
Ki-Young Kim ◽  
Andrew W. Truman ◽  
David E. Levin
Keyword(s):  
Cell Wall ◽  
Protein Kinase ◽  
Dna Binding ◽  
Transcriptional Activation ◽  
Kinase Activity ◽  
Wall Stress ◽  
Mitogen Activated Protein Kinase ◽  
Protein Kinase Activity ◽  
Mitogen Activated Protein

ABSTRACT The cell wall integrity mitogen-activated protein kinase (MAPK) cascade of Saccharomyces cerevisiae drives changes in gene expression in response to cell wall stress. We show that the MAPK of this pathway (Mpk1) and its pseudokinase paralog (Mlp1) use a noncatalytic mechanism to activate transcription of the FKS2 gene. Transcriptional activation of FKS2 was dependent on the Swi4/Swi6 (SBF) transcription factor and on an activating signal to Mpk1 but not on protein kinase activity. Activated (phosphorylated) Mpk1 and Mlp1 were detected in a complex with Swi4 and Swi6 at the FKS2 promoter. Mpk1 association with Swi4 in vivo required phosphorylation of Mpk1. Promoter association of Mpk1 and the Swi4 DNA-binding subunit of SBF were codependent but did not require Swi6, indicating that the MAPK confers DNA-binding ability to Swi4. Based on these data, we propose a model in which phosphorylated Mpk1 or Mlp1 forms a dimeric complex with Swi4 that is competent to associate with the FKS2 promoter. This complex then recruits Swi6 to activate transcription. Finally, we show that human ERK5, a functional ortholog of Mpk1, is similarly capable of driving FKS2 expression in the absence of protein kinase activity, suggesting that this mammalian MAPK may also have a noncatalytic function in vivo.

scholarly journals A Method for Assaying of Protein Kinase Activity In Vivo and Its Use in Studies of Signal Transduction in Strawberry Fruit Ripening

2021 ◽  
Vol 22 (19) ◽  
pp. 10495
Author(s):  
Wei Wang ◽  
Zhengrong Dai ◽  
Jie Li ◽  
Jinyao Ouyang ◽  
Tianyu Li ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Protein Kinase ◽  
Fruit Ripening ◽  
Kinase Activity ◽  
Expression Patterns ◽  
Protein Kinase Activity ◽  
Strawberry Fruit ◽  
Simple Method ◽  
Strawberry Fruit Ripening

Strawberry (Fragaria × ananassa) fruit ripening is regulated by a complex of cellular signal transduction networks, in which protein kinases are key components. Here, we report a relatively simple method for assaying protein kinase activity in vivo and specifically its application to study the kinase, FaMPK6, signaling in strawberry fruit. Green fluorescent protein (GFP)-tagged FaMPK6 was transiently expressed in strawberry fruit and after stimuli were applied to the fruit it was precipitated using an anti-GFP antibody. The precipitated kinase activity was measured in vitro using 32P-ATP and myelin basic protein (MBP) as substrates. We also report that FaMPK6 is not involved in the abscisic acid (ABA) signaling cascade, which is closely associated with FaMPK6 signaling in other plant species. However, methyl jasmonate (MeJA), low temperature, and high salt treatments were all found to activate FaMPK6. Transient manipulation of FaMPK6 expression was observed to cause significant changes in the expression patterns of 2749 genes, of which 264 were associated with MeJA signaling. The data also suggest a role for FaMPK6 in modulating cell wall metabolism during fruit ripening. Taken together, the presented method is powerful and its use will contribute to a profound exploration to the signaling mechanism of strawberry fruit ripening.

scholarly journals Interleukin-6 signals activating junB and TIS11 gene transcription in a B-cell hybridoma

1991 ◽  
Vol 11 (3) ◽  
pp. 1409-1418
Author(s):  
K Nakajima ◽  
R Wall
Keyword(s):  
Signal Transduction ◽  
Protein Kinase ◽  
B Cell ◽  
Tyrosine Phosphorylation ◽  
Gene Transcription ◽  
Interleukin 6 ◽  
Kinase Activity ◽  
Kinase Inhibitor ◽  
Primary Response ◽  
Protein Kinase Activity

The events in interleukin-6 (IL-6) signal transduction leading to primary response gene activation were analyzed in murine B-cell hybridoma and plasmacytoma cells which require IL-6 for growth. IL-6 stimulation of IL-6-deprived cells resulted in the rapid and transient tyrosine phosphorylation of a 160-kDa cellular protein (p160). This was followed by the highly selective induction of two primary response genes, junB/AP-1 transcription factor and TIS11. junB and TIS11 inductions were unaffected by cycloheximide, suggesting that posttranslational modifications accounted for their activation. Activation of junB and TIS11 transcription required rapid tyrosine kinase activity as well as a different protein kinase activity sensitive to the potent kinase inhibitor, H7, and activated following p160 tyrosine phosphorylation. This H7-sensitive kinase appears to be distinct from any well-characterized protein kinase-second messenger system. On the basis of these findings, we propose that IL-6-induced signal transduction proceeds through a novel protein kinase cascade which activates junB and TIS11 gene transcription.

scholarly journals Interleukin-6 signals activating junB and TIS11 gene transcription in a B-cell hybridoma.

1991 ◽  
Vol 11 (3) ◽  
pp. 1409-1418 ◽  
Author(s):  
K Nakajima ◽  
R Wall
Keyword(s):  
Signal Transduction ◽  
Protein Kinase ◽  
B Cell ◽  
Tyrosine Phosphorylation ◽  
Gene Transcription ◽  
Interleukin 6 ◽  
Kinase Activity ◽  
Kinase Inhibitor ◽  
Primary Response ◽  
Protein Kinase Activity

The events in interleukin-6 (IL-6) signal transduction leading to primary response gene activation were analyzed in murine B-cell hybridoma and plasmacytoma cells which require IL-6 for growth. IL-6 stimulation of IL-6-deprived cells resulted in the rapid and transient tyrosine phosphorylation of a 160-kDa cellular protein (p160). This was followed by the highly selective induction of two primary response genes, junB/AP-1 transcription factor and TIS11. junB and TIS11 inductions were unaffected by cycloheximide, suggesting that posttranslational modifications accounted for their activation. Activation of junB and TIS11 transcription required rapid tyrosine kinase activity as well as a different protein kinase activity sensitive to the potent kinase inhibitor, H7, and activated following p160 tyrosine phosphorylation. This H7-sensitive kinase appears to be distinct from any well-characterized protein kinase-second messenger system. On the basis of these findings, we propose that IL-6-induced signal transduction proceeds through a novel protein kinase cascade which activates junB and TIS11 gene transcription.

scholarly journals Serum-induced translocation of mitogen-activated protein kinase to the cell surface ruffling membrane and the nucleus

1993 ◽  
Vol 122 (5) ◽  
pp. 1089-1101 ◽  
Author(s):  
FA Gonzalez ◽  
A Seth ◽  
DL Raden ◽  
DS Bowman ◽  
FS Fay ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Protein Kinase ◽  
Cell Surface ◽  
Map Kinase ◽  
Map Kinases ◽  
Kinase Activity ◽  
Mitogen Activated Protein Kinase ◽  
Protein Kinase Activity ◽  
Mitogen Activated Protein ◽  
Cellular Compartments

The mitogen-activated protein (MAP) kinase signal transduction pathway represents an important mechanism by which growth factors regulate cell function. Targets of the MAP kinase pathway are located within several cellular compartments. Signal transduction therefore requires the localization of MAP kinase in each sub-cellular compartment that contains physiologically relevant substrates. Here, we show that serum treatment causes the translocation of two human MAP kinase isoforms, p40mapk and p41mapk, from the cytosol into the nucleus. In addition, we report that p41mapk (but not p40mapk) is localized at the cell surface ruffling membrane in serum-treated cells. To investigate whether the protein kinase activity of MAP kinase is required for serum-induced redistribution within the cell, we constructed mutated kinase-negative forms of p40mapk and p41mapk. The kinase-negative MAP kinases were not observed to localize to the cell surface ruffling membrane. In contrast, the kinase-negative MAP kinases were observed to be translocated to the nucleus. Intrinsic MAP kinase activity is therefore required only for localization at the cell surface and is not required for transport into the nucleus. Together, these data demonstrate that the pattern of serum-induced redistribution of p40mapk is different from p41mapk. Thus, in addition to common targets of signal transduction, it is possible that these MAP kinase isoforms may differentially regulate targets located in distinct sub-cellular compartments.

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