Structural basis of the correct subunit assembly, aggregation, and intracellular degradation of nylon hydrolase Article Swipe
Seiji Negoro
,
Naoki Shibata
,
Young-Ho Lee
,
Ikki Takehara
,
Ryo Kinugasa
,
Keisuke Nagai
,
Yusuke Tanaka
,
Dai‐ichiro Kato
,
Masahiro Takeo
,
Yuji Goto
,
Yoshiki Higuchi
·
YOU?
·
· 2018
· Open Access
·
· DOI: https://doi.org/10.1038/s41598-018-27860-w
YOU?
·
· 2018
· Open Access
·
· DOI: https://doi.org/10.1038/s41598-018-27860-w
Nylon hydrolase (NylC) is initially expressed as an inactive precursor (36 kDa). The precursor is cleaved autocatalytically at Asn266/Thr267 to generate an active enzyme composed of an α subunit (27 kDa) and a β subunit (9 kDa). Four αβ heterodimers (molecules A-D) form a doughnut-shaped quaternary structure. In this study, the thermostability of the parental NylC was altered by amino acid substitutions located at the A/D interface (D122G/H130Y/D36A/L137A) or the A/B interface (E263Q) and spanned a range of 47 °C. Considering structural, biophysical, and biochemical analyses, we discuss the structural basis of the stability of nylon hydrolase. From the analytical centrifugation data obtained regarding the various mutant enzymes, we conclude that the assembly of the monomeric units is dynamically altered by the mutations. Finally, we propose a model that can predict whether the fate of the nascent polypeptide will be correct subunit assembly, inappropriate protein-protein interactions causing aggregation, or intracellular degradation of the polypeptide.
Related Topics
Concepts
Protein subunit
Hydrolase
Thermostability
Protein quaternary structure
Intracellular
Biochemistry
Enzyme
Monomer
Chemistry
Mutant
Protein structure
Polymer
Organic chemistry
Gene
Metadata
- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1038/s41598-018-27860-w
- https://www.nature.com/articles/s41598-018-27860-w.pdf
- OA Status
- gold
- Cited By
- 16
- References
- 42
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W2809172793
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W2809172793Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.1038/s41598-018-27860-wDigital Object Identifier
- Title
-
Structural basis of the correct subunit assembly, aggregation, and intracellular degradation of nylon hydrolaseWork title
- Type
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articleOpenAlex work type
- Language
-
enPrimary language
- Publication year
-
2018Year of publication
- Publication date
-
2018-06-21Full publication date if available
- Authors
-
Seiji Negoro, Naoki Shibata, Young-Ho Lee, Ikki Takehara, Ryo Kinugasa, Keisuke Nagai, Yusuke Tanaka, Dai‐ichiro Kato, Masahiro Takeo, Yuji Goto, Yoshiki HiguchiList of authors in order
- Landing page
-
https://doi.org/10.1038/s41598-018-27860-wPublisher landing page
- PDF URL
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https://www.nature.com/articles/s41598-018-27860-w.pdfDirect link to full text PDF
- Open access
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YesWhether a free full text is available
- OA status
-
goldOpen access status per OpenAlex
- OA URL
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https://www.nature.com/articles/s41598-018-27860-w.pdfDirect OA link when available
- Concepts
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Protein subunit, Hydrolase, Thermostability, Protein quaternary structure, Intracellular, Biochemistry, Enzyme, Monomer, Chemistry, Mutant, Protein structure, Polymer, Organic chemistry, GeneTop concepts (fields/topics) attached by OpenAlex
- Cited by
-
16Total citation count in OpenAlex
- Citations by year (recent)
-
2025: 2, 2024: 8, 2023: 2, 2022: 2, 2020: 2Per-year citation counts (last 5 years)
- References (count)
-
42Number of works referenced by this work
- Related works (count)
-
10Other works algorithmically related by OpenAlex
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| abstract_inverted_index.(D122G/H130Y/D36A/L137A) | 68 |
| cited_by_percentile_year.max | 99 |
| cited_by_percentile_year.min | 94 |
| corresponding_author_ids | https://openalex.org/A5082713962 |
| countries_distinct_count | 1 |
| institutions_distinct_count | 11 |
| corresponding_institution_ids | https://openalex.org/I180941496 |
| citation_normalized_percentile.value | 0.45747623 |
| citation_normalized_percentile.is_in_top_1_percent | False |
| citation_normalized_percentile.is_in_top_10_percent | False |