Abstract
For many, “DNA mimic protein” (DMP) remains an unfamiliar term. The key feature of these proteins is their DNA-like shape and charge distribution, and they affect the activity of DNA-binding proteins by occupying their DNA-binding domains. Functionally, DMPs regulate mechanisms such as gene expression, restriction, and DNA repair as well as the nucleosome package. Although a few DMPs, such as phage uracil DNA glycosylase inhibitor (UGI) and overcome classical restriction (Ocr), were reported about 20 years ago, only a small number of DMPs have been studied to date. In 2014, we reviewed the functional and structural features of 16 DMPs that were known at the time. Now, seven new DMPs, namely anti-CRISPR suppressors AcrF2, AcrF10 and AcrIIA4, human immunodeficiency virus essential factor VPR, multi-functional inhibitor anti-restriction nuclease (Arn), translational regulator AbbA, and putative Z-DNA mimic MBD3, have been reported. In addition, further study of two previously known DMPs, DMP19 and SAUGI, increased our knowledge of their importance and function. Here, we discuss these updated results and address how several characteristics of the structure/sequence of DMPs (e.g. the DNA-like charge distribution and structural D/E-rich repeats) might someday be used to identify new DMPs using bioinformatic approach.
| Original language | English |
|---|---|
| Pages (from-to) | 539-548 |
| Number of pages | 10 |
| Journal | IUBMB Life |
| Volume | 71 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - May 1 2019 |
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Keywords
- DNA mimic protein
- DNA mimicking
- DNA-binding protein
- gene regulation
- inhibitors
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Genetics
- Clinical Biochemistry
- Cell Biology
Cite this
New paradigm of functional regulation by DNA mimic proteins : Recent updates. / Wang, Hao Ching; Chou, Chia Cheng; Hsu, Kai Cheng; Lee, Chi Hua; Wang, Andrew H.J.
In: IUBMB Life, Vol. 71, No. 5, 01.05.2019, p. 539-548.Research output: Contribution to journal › Review article
}
TY - JOUR
T1 - New paradigm of functional regulation by DNA mimic proteins
T2 - Recent updates
AU - Wang, Hao Ching
AU - Chou, Chia Cheng
AU - Hsu, Kai Cheng
AU - Lee, Chi Hua
AU - Wang, Andrew H.J.
PY - 2019/5/1
Y1 - 2019/5/1
N2 - For many, “DNA mimic protein” (DMP) remains an unfamiliar term. The key feature of these proteins is their DNA-like shape and charge distribution, and they affect the activity of DNA-binding proteins by occupying their DNA-binding domains. Functionally, DMPs regulate mechanisms such as gene expression, restriction, and DNA repair as well as the nucleosome package. Although a few DMPs, such as phage uracil DNA glycosylase inhibitor (UGI) and overcome classical restriction (Ocr), were reported about 20 years ago, only a small number of DMPs have been studied to date. In 2014, we reviewed the functional and structural features of 16 DMPs that were known at the time. Now, seven new DMPs, namely anti-CRISPR suppressors AcrF2, AcrF10 and AcrIIA4, human immunodeficiency virus essential factor VPR, multi-functional inhibitor anti-restriction nuclease (Arn), translational regulator AbbA, and putative Z-DNA mimic MBD3, have been reported. In addition, further study of two previously known DMPs, DMP19 and SAUGI, increased our knowledge of their importance and function. Here, we discuss these updated results and address how several characteristics of the structure/sequence of DMPs (e.g. the DNA-like charge distribution and structural D/E-rich repeats) might someday be used to identify new DMPs using bioinformatic approach.
AB - For many, “DNA mimic protein” (DMP) remains an unfamiliar term. The key feature of these proteins is their DNA-like shape and charge distribution, and they affect the activity of DNA-binding proteins by occupying their DNA-binding domains. Functionally, DMPs regulate mechanisms such as gene expression, restriction, and DNA repair as well as the nucleosome package. Although a few DMPs, such as phage uracil DNA glycosylase inhibitor (UGI) and overcome classical restriction (Ocr), were reported about 20 years ago, only a small number of DMPs have been studied to date. In 2014, we reviewed the functional and structural features of 16 DMPs that were known at the time. Now, seven new DMPs, namely anti-CRISPR suppressors AcrF2, AcrF10 and AcrIIA4, human immunodeficiency virus essential factor VPR, multi-functional inhibitor anti-restriction nuclease (Arn), translational regulator AbbA, and putative Z-DNA mimic MBD3, have been reported. In addition, further study of two previously known DMPs, DMP19 and SAUGI, increased our knowledge of their importance and function. Here, we discuss these updated results and address how several characteristics of the structure/sequence of DMPs (e.g. the DNA-like charge distribution and structural D/E-rich repeats) might someday be used to identify new DMPs using bioinformatic approach.
KW - DNA mimic protein
KW - DNA mimicking
KW - DNA-binding protein
KW - gene regulation
KW - inhibitors
UR - http://www.scopus.com/inward/record.url?scp=85058937852&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85058937852&partnerID=8YFLogxK
U2 - 10.1002/iub.1992
DO - 10.1002/iub.1992
M3 - Review article
AN - SCOPUS:85058937852
VL - 71
SP - 539
EP - 548
JO - IUBMB Life
JF - IUBMB Life
SN - 1521-6543
IS - 5
ER -