Microprotein: Difference between revisions
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== Function == | == Function == | ||
The function of microProteins is post-translational regulators. <ref name=":1" /> MicroProteins disrupt the formation of heterodimeric, homodimeric, or multimeric complexes. <ref name=":2" /> Furthermore, microProteins can interact with any protein that require functional dimers to function normally. <ref name=":1" /> The primary targets of microProteins are transcription factors that bind to DNA as dimers. <ref name=":1" /> MicroProteins regulate these complexes by creating homotypic dimers with the targets and inhibit protein complex function. <ref name=":1" /> There are two types of miP inhibitions: homotypic miP inhibition and heterotypic miP inhibition. <ref name=":2" /> In homotypic miP inhibition, microProteins interact with proteins with similar protein-protein interaction (PPI) domain. <ref name=":2" /> In heterotypic miP inhibition, microProteins interact with proteins with different but compatible PPI domain. <ref name=":2" /> In both types of inhibition, microProteins interfere and prevent the PPI domains from interacting with their normal proteins. <ref name=":2" /> | The function of microProteins is post-translational regulators. <ref name=":1" /> MicroProteins disrupt the formation of heterodimeric, homodimeric, or multimeric complexes. <ref name=":2" /> Furthermore, microProteins can interact with any protein that require functional dimers to function normally. <ref name=":1" /> The primary targets of microProteins are transcription factors that bind to DNA as dimers. <ref name=":1" /> MicroProteins regulate these complexes by creating homotypic dimers with the targets and inhibit protein complex function. <ref name=":1" /> There are two types of miP inhibitions: homotypic miP inhibition and heterotypic miP inhibition. <ref name=":2" /> In homotypic miP inhibition, microProteins interact with proteins with similar protein-protein interaction (PPI) domain. <ref name=":2" /> In heterotypic miP inhibition, microProteins interact with proteins with different but compatible PPI domain. <ref name=":2" /> In both types of inhibition, microProteins interfere and prevent the PPI domains from interacting with their normal proteins. <ref name=":2" /> | ||
== References == | |||
Revision as of 15:01, 25 April 2019
MicroProteins (miPs) are a class of protein with a single protein domain that are related to multidomain proteins. [1] MicroProteins regulate larger multidomain proteins at the post-translational level. [2] MicroProteins are analogous to microRNAs (miRNAs) and heterodimerize with their targets causing dominant and negative effects (Eguen). [3] In animals and plants, microProteins have been found to greatly influence the biological processes. [1] Because of microProteins dominant effects on their targets, microProteins are currently being studied for potential applications in biotechnology. [1]
History
The first microProtein (miP) discovered was during a research in the early 1990s on genes for basic helix–loop–helix (bHLH) transcription factors from a murine erythroleukaemia cell cDNA library. [2] The protein was found to be an inhibitor of DNA binding (Id), and it negatively regulate transcription factor complex. [2] The Id protein was 16 kDa and consisted of a helix-loop-helix (HLH) domain. [1] The microProtein formed bHLH/HLH heterodimers which disrupted the functional basic helix–loop–helix (bHLH) homodimers. [1] The first microProtein discovered in plants was the LITTLE ZIPPER (ZPR) protein. [1] The LTTLE ZIPPPER protein contains a leucine zipper domain but does not have the domains required for DNA binding and transcription activation. [1] Thus, LITTLE ZIPPER protein is analogous to the Id protein. [1] Despite not all proteins being small, in 2011, this class of protein was given the named microProteins because their negative regulatory actions are similar to those of miRNAs. [2]
Evolutionary, the Id protein or proteins similar to Id are found in all animals. [2] In plants, microProteins are only found in higher order. [2] However, the homeodomain transcription factors that belong to the three-amino-acid loop-extension (TALE) family are targets of microProteins, and this homeodomain proteins are conserved in animals, plants, and fungi. [2]
Structure
MicroProteins are generally small proteins with a single protein domain. [1] [3] However, not all microProteins are small, and the name was given because their actions are analogous to miRNAs. [2]
Function
The function of microProteins is post-translational regulators. [2] MicroProteins disrupt the formation of heterodimeric, homodimeric, or multimeric complexes. [3] Furthermore, microProteins can interact with any protein that require functional dimers to function normally. [2] The primary targets of microProteins are transcription factors that bind to DNA as dimers. [2] MicroProteins regulate these complexes by creating homotypic dimers with the targets and inhibit protein complex function. [2] There are two types of miP inhibitions: homotypic miP inhibition and heterotypic miP inhibition. [3] In homotypic miP inhibition, microProteins interact with proteins with similar protein-protein interaction (PPI) domain. [3] In heterotypic miP inhibition, microProteins interact with proteins with different but compatible PPI domain. [3] In both types of inhibition, microProteins interfere and prevent the PPI domains from interacting with their normal proteins. [3]
References
- ↑ 1.0 1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 Bhati, Kaushal Kumar; Blaakmeer, Anko; Paredes, Esther Botterweg; Dolde, Ulla; Eguen, Tenai; Hong, Shin-Young; Rodrigues, Vandasue; Straub, Daniel; et al. (2018-04-18). "Approaches to identify and characterize microProteins and their potential uses in biotechnology". Cellular and Molecular Life Sciences 75 (14): 2529–2536. doi:. ISSN 1420-682X. http://dx.doi.org/10.1007/s00018-018-2818-8.
- ↑ 2.00 2.01 2.02 2.03 2.04 2.05 2.06 2.07 2.08 2.09 2.10 2.11 Staudt, Annica-Carolin; Wenkel, Stephan (2010-12-10). "Regulation of protein function by ‘microProteins’". EMBO reports 12 (1): 35–42. doi:. ISSN 1469-221X. http://dx.doi.org/10.1038/embor.2010.196.
- ↑ 3.0 3.1 3.2 3.3 3.4 3.5 3.6 Eguen, T; Straub, D; Graeff, M; Wenkel, S (August 2015). "MicroProteins: small size-big impact". Trends in Plant Science 20 (8). doi:.