Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2018 Jul;75(14):2529-2536.
doi: 10.1007/s00018-018-2818-8. Epub 2018 Apr 18.

Approaches to identify and characterize microProteins and their potential uses in biotechnology

Affiliations
Review

Approaches to identify and characterize microProteins and their potential uses in biotechnology

Kaushal Kumar Bhati et al. Cell Mol Life Sci. 2018 Jul.

Abstract

MicroProteins are small proteins that contain a single protein domain and are related to larger, often multi-domain proteins. At the molecular level, microProteins act by interfering with the formation of higher order protein complexes. In the past years, several microProteins have been identified in plants and animals that strongly influence biological processes. Due to their ability to act as dominant regulators in a targeted manner, microProteins have a high potential for biotechnological use. In this review, we present different ways in which microProteins are generated and we elaborate on techniques used to identify and characterize them. Finally, we give an outlook on possible applications in biotechnology.

Keywords: Complex; Inhibition; MiPFinder; MicroProtein; Protein–protein interaction; Small proteins; Targets.

PubMed Disclaimer

Figures

Fig. 1
Fig. 1
Different modes of microProtein regulation. MicroProteins can act by (1) sequestering their targets into non-functional complexes, (2) by attracting chromatin repressor proteins (R), (3) by sequestering the target in a subcellular compartment where it is inactive, (4) by interacting with ion channel subunits and compromising their transport capacity
Fig. 2
Fig. 2
Two types of microProtein functions. MicroProtein interaction with its target and involved factors result in a stable repressed inactive form, here the system needs to be activated by certain factors to form an active complex. On the other hand, the target complex can be the active complex until the interaction of the microProtein with the target disturbs the stable target complex
Fig. 3
Fig. 3
Flowchart of microProtein identification and characterization

References

    1. Eguen T, Straub D, Graeff M, Wenkel S. MicroProteins: small size-big impact. Trends Plant Sci. 2015;20(8):477–482. doi: 10.1016/j.tplants.2015.05.011. - DOI - PubMed
    1. Graeff M, Wenkel S. Regulation of protein function by interfering protein species. Biomol Concepts. 2012;3(1):71–78. doi: 10.1515/bmc.2011.053. - DOI - PubMed
    1. Staudt AC, Wenkel S. Regulation of protein function by ‘microProteins’. EMBO Rep. 2011;12(1):35–42. doi: 10.1038/embor.2010.196. - DOI - PMC - PubMed
    1. Benezra R, Davis RL, Lockshon D, Turner DL, Weintraub H. The protein Id: a negative regulator of helix–loop–helix DNA binding proteins. Cell. 1990;61(1):49–59. doi: 10.1016/0092-8674(90)90214-Y. - DOI - PubMed
    1. Kim YS, Kim SG, Lee M, Lee I, Park HY, Seo PJ, Jung JH, Kwon EJ, Suh SW, Paek KH, Park CM. HD-ZIP III activity is modulated by competitive inhibitors via a feedback loop in Arabidopsis shoot apical meristem development. Plant Cell. 2008;20(4):920–933. doi: 10.1105/tpc.107.057448. - DOI - PMC - PubMed

Publication types

LinkOut - more resources