MicroProteins: Dynamic and accurate regulation of protein activity. Issue 4 (28th February 2022)
- Record Type:
- Journal Article
- Title:
- MicroProteins: Dynamic and accurate regulation of protein activity. Issue 4 (28th February 2022)
- Main Title:
- MicroProteins: Dynamic and accurate regulation of protein activity
- Authors:
- Wu, Qingqing
Zhong, Shangwei
Shi, Hui - Abstract:
- Abstract: Proteins usually assemble oligomers or high‐order complexes to increase their efficiency and specificity in biological processes. The dynamic equilibrium of complex formation and disruption imposes reversible regulation of protein function. MicroProteins are small, single‐domain proteins that directly bind target protein complexes and disrupt their assembly. Growing evidence shows that microProteins are efficient regulators of protein activity at the post‐translational level. In the last few decades, thousands of plant microProteins have been predicted by computational approaches, but only a few have been experimentally validated. Recent studies highlighted the mechanistic working modes of newly‐identified microProteins in Arabidopsis and other plant species. Here, we review characterized microProteins, including their biological roles, regulatory targets, and modes of action. In particular, we focus on microProtein‐directed allosteric modulation of key components in light signaling pathways, and we summarize the biogenesis and evolutionary trajectory of known microProteins in plants. Understanding the regulatory mechanisms of microProteins is an important step towards potential utilization of microProteins as versatile biotechnological tools in crop bioengineering. Abstract : Proteins often work as complexes through protein‐protein interactions. MicroProteins are small, single‐domain proteins that directly bind and fine‐tune the activity of target proteins. WeAbstract: Proteins usually assemble oligomers or high‐order complexes to increase their efficiency and specificity in biological processes. The dynamic equilibrium of complex formation and disruption imposes reversible regulation of protein function. MicroProteins are small, single‐domain proteins that directly bind target protein complexes and disrupt their assembly. Growing evidence shows that microProteins are efficient regulators of protein activity at the post‐translational level. In the last few decades, thousands of plant microProteins have been predicted by computational approaches, but only a few have been experimentally validated. Recent studies highlighted the mechanistic working modes of newly‐identified microProteins in Arabidopsis and other plant species. Here, we review characterized microProteins, including their biological roles, regulatory targets, and modes of action. In particular, we focus on microProtein‐directed allosteric modulation of key components in light signaling pathways, and we summarize the biogenesis and evolutionary trajectory of known microProteins in plants. Understanding the regulatory mechanisms of microProteins is an important step towards potential utilization of microProteins as versatile biotechnological tools in crop bioengineering. Abstract : Proteins often work as complexes through protein‐protein interactions. MicroProteins are small, single‐domain proteins that directly bind and fine‐tune the activity of target proteins. We summarize the biological roles and action modes of plant microProteins, and outline future directions for applications of microProteins as biotechnological tools in crop bioengineering. … (more)
- Is Part Of:
- Journal of integrative plant biology. Volume 64:Issue 4(2022)
- Journal:
- Journal of integrative plant biology
- Issue:
- Volume 64:Issue 4(2022)
- Issue Display:
- Volume 64, Issue 4 (2022)
- Year:
- 2022
- Volume:
- 64
- Issue:
- 4
- Issue Sort Value:
- 2022-0064-0004-0000
- Page Start:
- 812
- Page End:
- 820
- Publication Date:
- 2022-02-28
- Subjects:
- allosteric deactivation -- biotechnological tools -- light signaling -- MicroProteins -- post‐translational regulation
Plants -- Periodicals
Plants -- China -- Periodicals
Electronic journals
580.5 - Journal URLs:
- http://bibpurl.oclc.org/web/10380 ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1744-7909 ↗
http://www.blackwell-synergy.com/loi/jipb ↗
http://www.blackwell-synergy.com/openurl?genre=journal&eissn=1744-7909 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/jipb.13229 ↗
- Languages:
- English
- ISSNs:
- 1672-9072
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5007.538427
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 21292.xml