Microprotein: Difference between revisions
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{{for|a similar (if not identical) concept|Micropeptide}} | {{for|a similar (if not identical) concept|Micropeptide}} | ||
A '''microprotein''' (miP) is a small [[protein]] encoded from a [[small open reading frame]] (sORF),<ref name=":3">{{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> also known as '''sORF-encoded protein''' ('''SEP'''). They are a class of protein with a single [[protein domain]] | A '''microprotein''' (miP) is a small [[protein]] encoded from a [[small open reading frame]] (sORF),<ref name=":3">{{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> also known as '''sORF-encoded protein''' ('''SEP'''). They are a class of protein with a single [[protein domain]]. They are related to multidomain proteins.<ref name=":0">{{Cite journal|last1=Bhati|first1=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|journal=Cellular and Molecular Life Sciences|volume=75|issue=14|pages=2529–2536|doi=10.1007/s00018-018-2818-8|pmid=29670998|pmc=6003976|issn=1420-682X}}</ref> Microproteins regulate larger multidomain proteins at the post-translational level.<ref name=":1">{{Cite journal|last1=Staudt|first1=Annica-Carolin|last2=Wenkel|first2=Stephan|date=2010-12-10|title=Regulation of protein function by 'microProteins'|journal=EMBO Reports|volume=12|issue=1|pages=35–42|doi=10.1038/embor.2010.196|pmid=21151039|pmc=3024132|issn=1469-221X}}</ref> Microproteins are analogous to [[MicroRNA|microRNAs]] (miRNAs) and [[Protein dimer|heterodimerize]] with their targets causing dominant and negative effects.<ref name=":2">{{Cite journal|last1=Eguen|first1=T|last2=Straub|first2=D|last3=Graeff|first3=M|last4=Wenkel|first4=S|date=August 2015|title=MicroProteins: small size-big impact|journal=Trends in Plant Science|volume=20|issue=8|pages=477–482|doi=10.1016/j.tplants.2015.05.011|pmid=26115780|bibcode=2015TPS....20..477E}}</ref> In animals and plants, microproteins influence many biological processes.<ref name=":0" /> Because of their dominant effects on their targets, microproteins are currently under study for use in biotechnology.<ref name=":0" /> | ||
== History == | == History == | ||
The first | The first miP was discovered during a research in the early 1990s on genes for [[Basic helix-loop-helix|basic helix–loop–helix]] (bHLH) [[Transcription factor|transcription factors]] from a [[Murinae|murine]] [[Acute erythroid leukemia|erythroleukaemia]] cell [[cDNA library]].<ref name=":1" /> The protein was an [[Inhibitor of DNA-binding protein|inhibitor of DNA binding]] (ID protein), and negatively regulated the transcription factor complex.<ref name=":1" /> The protein was 16 kDa and consisted of a helix-loop-helix (HLH) domain.<ref name=":0" /> The microprotein formed bHLH/HLH heterodimers that disrupted the functional basic helix–loop–helix (bHLH) homodimers.<ref name=":0" /> | ||
The first microprotein discovered | The first plant microprotein discovered was the LITTLE ZIPPER (ZPR) protein.<ref name=":0" /> The LITTLE ZIPPER protein contains a [[leucine zipper]] domain, but lacks the domains required for DNA binding and transcription activation.<ref name=":0" /> Thus, LITTLE ZIPPER protein is analogous to the ID protein.<ref name=":0" /> Although not all proteins are small, in 2011, this class of protein was given the name microproteins because their negative regulatory actions are similar to those of miRNAs.<ref name=":1" /> | ||
The ID protein or proteins similar to ID are found in all animals.<ref name=":1" /> Plant microproteins are only found in higher orders.<ref name=":1" /> However, the [[homeodomain]] transcription factors that belong to the three-amino-acid loop-extension (TALE) family are targets of microproteins, and these homeodomain proteins are conserved in animals, plants, and fungi.<ref name=":1" /> | |||
== Structure == | == Structure == | ||
Microproteins | Microproteins generally feature a single protein domain.<ref name=":0" /><ref name=":2" /> The active form is translated from smORF.<ref name=":3" /> smORF codons can be less than 100 codons.<ref name=":3" /> However, not all microproteins are small, and the name was given because of the analogy to miRNAs.<ref name=":1" /> | ||
== Function == | == Function == | ||
Microproteins function as [[Post-translational regulation|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 requires functional dimers to function normally.<ref name=":1" /> The primary targets are transcription factors that bind to DNA as dimers.<ref>{{Cite journal|last1=de Klein|first1=Niek|last2=Magnani|first2=Enrico|last3=Banf|first3=Michael|last4=Rhee|first4=Seung Yon|date=2015|title=microProtein Prediction Program (miP3): A Software for Predicting microProteins and Their Target Transcription Factors|journal=International Journal of Genomics|volume=2015|pages=734147|doi=10.1155/2015/734147|pmid=26060811|pmc=4427850|issn=2314-436X|doi-access=free}}</ref><ref name=":1" /> Microproteins regulate these complexes by creating homotypic dimers with the targets and inhibit protein complex function.<ref name=":1" /> The two types of miP inhibitions are: 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 04:13, 17 August 2025
Template:For A microprotein (miP) is a small protein encoded from a small open reading frame (sORF),[1] also known as sORF-encoded protein (SEP). They are a class of protein with a single protein domain. They 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.[4] In animals and plants, microproteins influence many biological processes.[2] Because of their dominant effects on their targets, microproteins are currently under study for use in biotechnology.[2]
History
The first miP was discovered 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 an inhibitor of DNA binding (ID protein), and negatively regulated the transcription factor complex.[3] The protein was 16 kDa and consisted of a helix-loop-helix (HLH) domain.[2] The microprotein formed bHLH/HLH heterodimers that disrupted the functional basic helix–loop–helix (bHLH) homodimers.[2]
The first plant microprotein discovered was the LITTLE ZIPPER (ZPR) protein.[2] The LITTLE ZIPPER protein contains a leucine zipper domain, but lacks the domains required for DNA binding and transcription activation.[2] Thus, LITTLE ZIPPER protein is analogous to the ID protein.[2] Although not all proteins are small, in 2011, this class of protein was given the name microproteins because their negative regulatory actions are similar to those of miRNAs.[3]
The ID protein or proteins similar to ID are found in all animals.[3] Plant microproteins are only found in higher orders.[3] However, the homeodomain transcription factors that belong to the three-amino-acid loop-extension (TALE) family are targets of microproteins, and these homeodomain proteins are conserved in animals, plants, and fungi.[3]
Structure
Microproteins generally feature a single protein domain.[2][4] The active form is translated from smORF.[1] smORF codons can be less than 100 codons.[1] However, not all microproteins are small, and the name was given because of the analogy to miRNAs.[3]
Function
Microproteins function as post-translational regulators.[3] Microproteins disrupt the formation of heterodimeric, homodimeric, or multimeric complexes.[4] Furthermore, microproteins can interact with any protein that requires functional dimers to function normally.[3] The primary targets are transcription factors that bind to DNA as dimers.[5][3] Microproteins regulate these complexes by creating homotypic dimers with the targets and inhibit protein complex function.[3] The two types of miP inhibitions are: 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
- ↑ 1.0 1.1 1.2 "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. PMID 29670998.
- ↑ 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. PMID 21151039.
- ↑ 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): 477–482. doi:. PMID 26115780. Bibcode: 2015TPS....20..477E.
- ↑ de Klein, Niek; Magnani, Enrico; Banf, Michael; Rhee, Seung Yon (2015). "microProtein Prediction Program (miP3): A Software for Predicting microProteins and Their Target Transcription Factors". International Journal of Genomics 2015: 734147. doi:. ISSN 2314-436X. PMID 26060811.