IdeaWazaWiki - User contributions [en]

Microprotein

2022-09-23T19:52:20Z

24.255.102.172: /* History */

{{orphan|date=April 2019}}

A '''microprotein''' (miP) is a small [[protein]] encoded from small [[open reading frame]] (smORF).<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> They are a class of protein with a single [[protein domain]] that 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 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}}</ref> In animals and plants, microproteins have been found to greatly influence 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 ==
The first microprotein (miP) discovered was 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 murine erythroleukaemia cell [[cDNA library]].<ref name=":1" /> The protein was found to be an inhibitor of DNA binding (Id), and it negatively regulate transcription factor complex.<ref name=":1" /> The Id protein was 16 kDa and consisted of a helix-loop-helix (HLH) domain.<ref name=":0" /> The microprotein formed bHLH/HLH heterodimers which disrupted the functional basic helix–loop–helix (bHLH) homodimers.<ref name=":0" /> The first microprotein discovered in plants was the LITTLE ZIPPER (ZPR) protein.<ref name=":0" /> The LITTLE ZIPPER protein contains a [[leucine zipper]] domain but does not have 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" /> Despite not all proteins being 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" />

Evolutionarily, the Id protein or proteins similar to Id found in all animals.<ref name=":1" /> In plants, microproteins are only found in higher order.<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 ==
Microproteins are generally small proteins with a single protein domain.<ref name=":0" /><ref name=":2" /> The active form of microproteins are translated from smORF.<ref name=":3" /> The smORF codons which microproteins are translated from can be less than 100 codons.<ref name=":3" /> However, not all microproteins are small, and the name was given because their actions are analogous to miRNAs.<ref name=":1" />

== Function ==
The function of microproteins is [[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 require functional dimers to function normally.<ref name=":1" /> The primary targets of microproteins 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" /> 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 />

[[Category:Protein classification]]
[[Category:Post-translational modification]]

Microprotein

2022-09-23T19:49:47Z

24.255.102.172: /* History */

{{orphan|date=April 2019}}

A '''microprotein''' (miP) is a small [[protein]] encoded from small [[open reading frame]] (smORF).<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> They are a class of protein with a single [[protein domain]] that 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 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}}</ref> In animals and plants, microproteins have been found to greatly influence 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 ==
The first microprotein (miP) discovered was 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 murine erythroleukaemia cell [[cDNA library]].<ref name=":1" /> The protein was found to be an inhibitor of DNA binding (Id), and it negatively regulate transcription factor complex.<ref name=":1" /> The Id protein was 16 kDa and consisted of a helix-loop-helix (HLH) domain.<ref name=":0" /> The microprotein formed bHLH/HLH heterodimers which disrupted the functional basic helix–loop–helix (bHLH) homodimers.<ref name=":0" /> The first microprotein discovered in plants was the LITTLE ZIPPER (ZPR) protein.<ref name=":0" /> The LITTLE ZIPPER protein contains a [[leucine zipper]] domain but does not have 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" /> 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.<ref name=":1" />

Evolutionary, the Id protein or proteins similar to Id are found in all animals.<ref name=":1" /> In plants, microproteins are only found in higher order.<ref name=":1" /> 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.<ref name=":1" />

== Structure ==
Microproteins are generally small proteins with a single protein domain.<ref name=":0" /><ref name=":2" /> The active form of microproteins are translated from smORF.<ref name=":3" /> The smORF codons which microproteins are translated from can be less than 100 codons.<ref name=":3" /> However, not all microproteins are small, and the name was given because their actions are analogous to miRNAs.<ref name=":1" />

== Function ==
The function of microproteins is [[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 require functional dimers to function normally.<ref name=":1" /> The primary targets of microproteins 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" /> 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 />

[[Category:Protein classification]]
[[Category:Post-translational modification]]