Microprotein: Difference between revisions
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Microproteins (miPs) are a class of protein with a single protein domain that are related to multidomain proteins. <ref name=":0">{{Cite journal|last=Bhati|first=Kaushal Kumar|last2=Blaakmeer|first2=Anko|last3=Paredes|first3=Esther Botterweg|last4=Dolde|first4=Ulla|last5=Eguen|first5=Tenai|last6=Hong|first6=Shin-Young|last7=Rodrigues|first7=Vandasue|last8=Straub|first8=Daniel|last9=Sun|first9=Bin|date=2018-04-18|title=Approaches to identify and characterize microProteins and their potential uses in biotechnology|url=http://dx.doi.org/10.1007/s00018-018-2818-8|journal=Cellular and Molecular Life Sciences|volume=75|issue=14|pages=2529–2536|doi=10.1007/s00018-018-2818-8|issn=1420-682X}}</ref> Microproteins regulate larger multidomain proteins at the post-translational level. <ref name=":1">{{Cite journal|last=Staudt|first=Annica-Carolin|last2=Wenkel|first2=Stephan|date=2010-12-10|title=Regulation of protein function by ‘microProteins’|url=http://dx.doi.org/10.1038/embor.2010.196|journal=EMBO reports|volume=12|issue=1|pages=35–42|doi=10.1038/embor.2010.196|issn=1469-221X}}</ref> Microproteins are analogous to microRNAs | Microproteins (miPs) are small proteins encoded by small open reading frame (smORF). <ref>{{Cite web|url=https://www.the-scientist.com/features/the-dark-matter-of-the-human-proteome-65628|title=The Dark Matter of the Human Proteome|website=The Scientist Magazine®|language=en|access-date=2019-04-25}}</ref> They are a class of protein with a single protein domain that are related to multidomain proteins. <ref name=":0">{{Cite journal|last=Bhati|first=Kaushal Kumar|last2=Blaakmeer|first2=Anko|last3=Paredes|first3=Esther Botterweg|last4=Dolde|first4=Ulla|last5=Eguen|first5=Tenai|last6=Hong|first6=Shin-Young|last7=Rodrigues|first7=Vandasue|last8=Straub|first8=Daniel|last9=Sun|first9=Bin|date=2018-04-18|title=Approaches to identify and characterize microProteins and their potential uses in biotechnology|url=http://dx.doi.org/10.1007/s00018-018-2818-8|journal=Cellular and Molecular Life Sciences|volume=75|issue=14|pages=2529–2536|doi=10.1007/s00018-018-2818-8|issn=1420-682X}}</ref> Microproteins regulate larger multidomain proteins at the post-translational level. <ref name=":1">{{Cite journal|last=Staudt|first=Annica-Carolin|last2=Wenkel|first2=Stephan|date=2010-12-10|title=Regulation of protein function by ‘microProteins’|url=http://dx.doi.org/10.1038/embor.2010.196|journal=EMBO reports|volume=12|issue=1|pages=35–42|doi=10.1038/embor.2010.196|issn=1469-221X}}</ref> Microproteins are analogous to microRNAs (miRNAs) and heterodimerize with their targets causing dominant and negative effects (Eguen). <ref name=":2">{{Cite journal|last=Eguen|first=T|last2=Straub|first2=D|last3=Graeff|first3=M|last4=Wenkel|first4=S|date=August 2015|title=MicroProteins: small size-big impact|url=|journal=Trends in Plant Science|volume=20|issue=8|pages=|doi=10.1016/j.tplants.2015.05.011|via=}}</ref> In animals and plants, microproteins have been found to greatly influence the biological processes. <ref name=":0" /> Because of microproteins dominant effects on their targets, microproteins are currently being studied for potential applications in biotechnology. <ref name=":0" /> | ||
== History == | == History == | ||
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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 == | == References == | ||
Revision as of 22:54, 25 April 2019
Microproteins (miPs) are small proteins encoded by small open reading frame (smORF). [1] They are a class of protein with a single protein domain that are related to multidomain proteins. [2] Microproteins regulate larger multidomain proteins at the post-translational level. [3] Microproteins are analogous to microRNAs (miRNAs) and heterodimerize with their targets causing dominant and negative effects (Eguen). [4] In animals and plants, microproteins have been found to greatly influence the biological processes. [2] Because of microproteins dominant effects on their targets, microproteins are currently being studied for potential applications in biotechnology. [2]
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. [3] The protein was found to be an inhibitor of DNA binding (Id), and it negatively regulate transcription factor complex. [3] The Id protein was 16 kDa and consisted of a helix-loop-helix (HLH) domain. [2] The microprotein formed bHLH/HLH heterodimers which disrupted the functional basic helix–loop–helix (bHLH) homodimers. [2] The first microprotein discovered in plants was the LITTLE ZIPPER (ZPR) protein. [2] The LTTLE ZIPPPER protein contains a leucine zipper domain but does not have the domains required for DNA binding and transcription activation. [2] Thus, LITTLE ZIPPER protein is analogous to the Id protein. [2] 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. [3]
Evolutionary, the Id protein or proteins similar to Id are found in all animals. [3] In plants, microproteins are only found in higher order. [3] 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. [3]
Structure
Microproteins are generally small proteins with a single protein domain. [2] [4] However, not all microproteins are small, and the name was given because their actions are analogous to miRNAs. [3]
Function
The function of microproteins is post-translational regulators. [3] Microproteins disrupt the formation of heterodimeric, homodimeric, or multimeric complexes. [4] Furthermore, microproteins can interact with any protein that require functional dimers to function normally. [3] The primary targets of microproteins are transcription factors that bind to DNA as dimers. [3] Microproteins regulate these complexes by creating homotypic dimers with the targets and inhibit protein complex function. [3] There are two types of miP inhibitions: homotypic miP inhibition and heterotypic miP inhibition. [4] In homotypic miP inhibition, microproteins interact with proteins with similar protein-protein interaction (PPI) domain. [4] In heterotypic miP inhibition, microproteins interact with proteins with different but compatible PPI domain. [4] In both types of inhibition, microproteins interfere and prevent the PPI domains from interacting with their normal proteins. [4]
References
- ↑ "The Dark Matter of the Human Proteome" (in en). https://www.the-scientist.com/features/the-dark-matter-of-the-human-proteome-65628.
- ↑ 2.0 2.1 2.2 2.3 2.4 2.5 2.6 2.7 2.8 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.
- ↑ 3.00 3.01 3.02 3.03 3.04 3.05 3.06 3.07 3.08 3.09 3.10 3.11 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.
- ↑ 4.0 4.1 4.2 4.3 4.4 4.5 4.6 Eguen, T; Straub, D; Graeff, M; Wenkel, S (August 2015). "MicroProteins: small size-big impact". Trends in Plant Science 20 (8). doi:.
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