Search
- Page Path
-
HOME
> Search
Review
- [Minireview]Biodegradation of plastics: mining of plastic-degrading microorganisms and enzymes using metagenomics approaches
-
Dae-Wi Kim , Jae-Hyung Ahn , Chang-Jun Cha
-
J. Microbiol. 2022;60(10):969-976. Published online September 27, 2022
-
DOI: https://doi.org/10.1007/s12275-022-2313-7
-
-
18
View
-
0
Download
-
17
Citations
-
Abstract
- Plastic pollution exacerbated by the excessive use of synthetic
plastics and its recalcitrance has been recognized among the
most pressing global threats. Microbial degradation of plastics
has gained attention as a possible eco-friendly countermeasure,
as several studies have shown microbial metabolic
capabilities as potential degraders of various synthetic plastics.
However, still defined biochemical mechanisms of biodegradation
for the most plastics remain elusive, because the
widely used culture-dependent approach can access only a
very limited amount of the metabolic potential in each microbiome.
A culture-independent approach, including metagenomics,
is becoming increasingly important in the mining
of novel plastic-degrading enzymes, considering its more expanded
coverage on the microbial metabolism in microbiomes.
Here, we described the advantages and drawbacks associated
with four different metagenomics approaches (microbial community
analysis, functional metagenomics, targeted gene sequencing,
and whole metagenome sequencing) for the mining
of plastic-degrading microorganisms and enzymes from
the plastisphere. Among these approaches, whole metagenome
sequencing has been recognized among the most powerful
tools that allow researchers access to the entire metabolic potential
of a microbiome. Accordingly, we suggest strategies
that will help to identify plastisphere-enriched sequences as
de novo plastic-degrading enzymes using the whole metagenome
sequencing approach. We anticipate that new strategies
for metagenomics approaches will continue to be developed
and facilitate to identify novel plastic-degrading microorganisms
and enzymes from microbiomes.
Journal Article
- Structural and biochemical analysis of the PTPN4 PDZ domain bound to the C-terminal tail of the human papillomavirus E6 oncoprotein
-
Hye Seon Lee , Hye-Yeoung Yun , Eun-Woo Lee , Ho-Chul Shin , Seung Jun Kim , Bonsu Ku
-
J. Microbiol. 2022;60(4):395-401. Published online January 28, 2022
-
DOI: https://doi.org/10.1007/s12275-022-1606-1
-
-
19
View
-
0
Download
-
6
Citations
-
Abstract
- High-risk genotypes of human papillomaviruses (HPVs) are
directly implicated in various abnormalities associated with
cellular hyperproliferation, including cervical cancer. E6 is one
of two oncoproteins encoded in the HPV genome, which recruits
diverse PSD-95/Dlg/ZO-1 (PDZ) domain-containing
human proteins through its C-terminal PDZ-binding motif
(PBM) to be degraded by means of the proteasome pathway.
Among the three PDZ domain-containing protein tyrosine
phosphatases, protein tyrosine phosphatase non-receptor type
3 (PTPN3) and PTPN13 were identified to be recognized by
HPV E6 in a PBM-dependent manner. However, whether
HPV E6 associates with PTPN4, which also has a PDZ domain
and functions as an apoptosis regulator, remains undetermined.
Herein, we present structural and biochemical evidence
demonstrating the direct interaction between the PBM
of HPV16 E6 and the PDZ domain of human PTPN4 for the
first time. X-ray crystallographic structure determination and
binding measurements using isothermal titration calorimetry
demonstrated that hydrophobic interactions in which Leu158
of HPV16 E6 plays a key role and a network of intermolecular
hydrogen bonds sustain the complex formation between
PTPN4 PDZ and the PBM of HPV16 E6. In addition, it was
verified that the corresponding motifs from several other highrisk
HPV genotypes, including HPV18, HPV31, HPV33, and
HPV45, bind to PTPN4 PDZ with comparable affinities, suggesting
that PTPN4 is a common target of various pathogenic
HPV genotypes.
TOP