2023
DOI: 10.1016/j.heliyon.2023.e18916
|View full text |Cite
|
Sign up to set email alerts
|

Identification of a putative kinase interacting domain in the durum wheat catalase 1 (TdCAT1) protein

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3

Citation Types

0
3
0

Year Published

2023
2023
2024
2024

Publication Types

Select...
3

Relationship

2
1

Authors

Journals

citations
Cited by 3 publications
(3 citation statements)
references
References 63 publications
0
3
0
Order By: Relevance
“…Interestingly, the catalase activity of TdCAT1 increased gradually with increasing concentrations of cations in the medium, with the most important effect being enregistered in the presence of Fe 2+ and Mn 2+ [13]. In addition, those proteins can interact with other proteins, as previously described, such as the CaM/Ca 2+ complex [13] and protein kinases [62]. In addition, AvCAT1/2 and 3 are structural constituents of ribosomes, whereas AvCAT1/2 /3 and 5 have 5S rRNA binding functions (Figure 6).…”
Section: Discussionmentioning
confidence: 51%
See 1 more Smart Citation
“…Interestingly, the catalase activity of TdCAT1 increased gradually with increasing concentrations of cations in the medium, with the most important effect being enregistered in the presence of Fe 2+ and Mn 2+ [13]. In addition, those proteins can interact with other proteins, as previously described, such as the CaM/Ca 2+ complex [13] and protein kinases [62]. In addition, AvCAT1/2 and 3 are structural constituents of ribosomes, whereas AvCAT1/2 /3 and 5 have 5S rRNA binding functions (Figure 6).…”
Section: Discussionmentioning
confidence: 51%
“…In fact, treatment of TdCAT1 by phosphatase inhibited the catalytic activity of the protein [14]. Interestingly, it has been recently shown that TdCAT1 proteins could be phosphorylated in vitro in the presence of wheat Mitogen-Activated Protein Kinase protein (TMPK3) and that the presence of TMPK3 enhanced the catalytic activity of the catalase [62]. In the current work, in silico analyses showed that AvCAT proteins could be phosphorylated by MAPKs.…”
Section: Discussionmentioning
confidence: 65%
“…A recent study has shown that the catalase activity of durum wheat catalase (TdCAT1) was hindered following protein dephosphorylation through treatment with λ-phosphatase [ 61 ]. In addition, TdCAT1 interacts with mitogen-activated protein kinase 3 (TMPK3) through its N-terminal region and enhances its catalytic activity [ 62 ]. Our analysis in this study revealed that MAPKs can phosphorylate CAT proteins.…”
Section: Discussionmentioning
confidence: 99%