The Moonlighting Function of Soybean Disordered Methyl-CpG-Binding Domain 10c Protein

Intrinsically disordered proteins (IDPs) are multifunctional due to their ability to adopt different structures depending on the local conditions. The intrinsically disordered regions of methyl-CpG-binding domain (MBD) proteins play important roles in regulating growth and development by interpretin...

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Bibliographic Details
Published in:International journal of molecular sciences 2023-05, Vol.24 (10), p.8677
Main Authors: Li, Yanling, Qin, Jiawei, Chen, Menglu, Sun, Nan, Tan, Fangmei, Zhang, Hua, Zou, Yongdong, Uversky, Vladimir N, Liu, Yun
Format: Article
Language:English
Subjects:
Amino acids
Binding
Cell cycle
Circular dichroism
Dichroism
DNA Methylation
Enzymatic activity
Enzyme activity
Enzymes
Escherichia coli
Freeze-thawing
Genes
Glycine max - genetics
Glycine max - metabolism
Heat stress
Intrinsically Disordered Proteins - chemistry
L-Lactate dehydrogenase
L-Lactate Dehydrogenase - metabolism
Lactate dehydrogenase
Methylation
NMR
Nuclear magnetic resonance
Phylogenetics
Protein binding
Proteins
Salinity tolerance
Signal transduction
Soybean
Soybeans
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Summary:Intrinsically disordered proteins (IDPs) are multifunctional due to their ability to adopt different structures depending on the local conditions. The intrinsically disordered regions of methyl-CpG-binding domain (MBD) proteins play important roles in regulating growth and development by interpreting DNA methylation patterns. However, whether MBDs have a stress-protective function is far from clear. In this paper, soybean GmMBD10c protein, which contains an MBD and is conserved in Leguminosae, was predicted to be located in the nucleus. It was found to be partially disordered by bioinformatic prediction, circular dichroism and a nuclear magnetic resonance spectral analysis. The enzyme activity assay and SDS-PAGE results showed that GmMBD10c can protect lactate dehydrogenase and a broad range of other proteins from misfolding and aggregation induced by the freeze-thaw process and heat stress, respectively. Furthermore, overexpression of GmMBD10c enhanced the salt tolerance of . These data validate that GmMBD10c is a moonlighting protein with multiple functions.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms24108677