Distinct Contributions of Tryptophan Residues within the Dimerization Domain to Nanog Function Article Swipe
Nicholas P. Mullin
,
Alessia Gagliardi
,
Le Tran Phuc Khoa
,
Douglas Colby
,
Elisa Hall-Ponselé
,
Arthur J. Rowe
,
Ian Chambers
·
YOU?
·
· 2016
· Open Access
·
· DOI: https://doi.org/10.1016/j.jmb.2016.12.001
YOU?
·
· 2016
· Open Access
·
· DOI: https://doi.org/10.1016/j.jmb.2016.12.001
The level of the transcription factor Nanog directly determines the efficiency of mouse embryonic stem cell self-renewal. Nanog protein exists as a dimer with the dimerization domain composed of a simple repeat region in which every fifth residue is a tryptophan, the tryptophan repeat (WR). Although WR is necessary to enable Nanog to confer LIF-independent self-renewal, the mechanism of dimerization and the effect of modulating dimerization strength have been unclear. Here we couple mutagenesis with functional and dimerization assays to show that the number of tryptophans within the WR is linked to the strength of homodimerization, Sox2 heterodimerization and self-renewal activity. A reduction in the number of tryptophan residues leads initially to a gradual reduction in activity before a precipitous reduction in activity occurs upon reduction in tryptophan number below eight. Further functional attrition follows subsequent tryptophan number reduction with substitution of all tryptophan residues ablating dimerization and self-renewal function completely. A strong positional influence of tryptophans exists, with residues at the WR termini contributing more to Nanog function, particularly at the N-terminal end. Limited proteolysis demonstrates that a structural core of Nanog encompassing the homeodomain and the tryptophan repeat can support LIF-independent colony formation. These results increase understanding of the molecular interactions occurring between transcription factor subunits at the core of the pluripotency gene regulatory network and will enhance our ability to control pluripotent cell self-renewal and differentiation.
Related Topics
Concepts
Homeobox protein NANOG
Tryptophan
Transcription factor
Cell biology
Biology
Chemistry
SOX2
Biochemistry
Embryonic stem cell
Induced pluripotent stem cell
Gene
Amino acid
Metadata
- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1016/j.jmb.2016.12.001
- OA Status
- hybrid
- Cited By
- 17
- References
- 34
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W2559947108
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W2559947108Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.1016/j.jmb.2016.12.001Digital Object Identifier
- Title
-
Distinct Contributions of Tryptophan Residues within the Dimerization Domain to Nanog FunctionWork title
- Type
-
articleOpenAlex work type
- Language
-
enPrimary language
- Publication year
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2016Year of publication
- Publication date
-
2016-12-06Full publication date if available
- Authors
-
Nicholas P. Mullin, Alessia Gagliardi, Le Tran Phuc Khoa, Douglas Colby, Elisa Hall-Ponselé, Arthur J. Rowe, Ian ChambersList of authors in order
- Landing page
-
https://doi.org/10.1016/j.jmb.2016.12.001Publisher landing page
- Open access
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YesWhether a free full text is available
- OA status
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hybridOpen access status per OpenAlex
- OA URL
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https://doi.org/10.1016/j.jmb.2016.12.001Direct OA link when available
- Concepts
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Homeobox protein NANOG, Tryptophan, Transcription factor, Cell biology, Biology, Chemistry, SOX2, Biochemistry, Embryonic stem cell, Induced pluripotent stem cell, Gene, Amino acidTop concepts (fields/topics) attached by OpenAlex
- Cited by
-
17Total citation count in OpenAlex
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2025: 2, 2023: 2, 2021: 2, 2020: 5, 2019: 1Per-year citation counts (last 5 years)
- References (count)
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34Number of works referenced by this work
- Related works (count)
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10Other works algorithmically related by OpenAlex
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| abstract_inverted_index.determines | 8 |
| abstract_inverted_index.efficiency | 10 |
| abstract_inverted_index.formation. | 194 |
| abstract_inverted_index.functional | 75, 132 |
| abstract_inverted_index.modulating | 64 |
| abstract_inverted_index.positional | 153 |
| abstract_inverted_index.regulatory | 215 |
| abstract_inverted_index.structural | 179 |
| abstract_inverted_index.subsequent | 135 |
| abstract_inverted_index.tryptophan | 42, 107, 127, 136, 143, 188 |
| abstract_inverted_index.completely. | 150 |
| abstract_inverted_index.homeodomain | 185 |
| abstract_inverted_index.mutagenesis | 73 |
| abstract_inverted_index.pluripotent | 224 |
| abstract_inverted_index.precipitous | 119 |
| abstract_inverted_index.proteolysis | 175 |
| abstract_inverted_index.tryptophan, | 40 |
| abstract_inverted_index.tryptophans | 85, 156 |
| abstract_inverted_index.contributing | 164 |
| abstract_inverted_index.demonstrates | 176 |
| abstract_inverted_index.dimerization | 25, 59, 65, 77, 146 |
| abstract_inverted_index.encompassing | 183 |
| abstract_inverted_index.interactions | 202 |
| abstract_inverted_index.particularly | 169 |
| abstract_inverted_index.pluripotency | 213 |
| abstract_inverted_index.self-renewal | 99, 148, 226 |
| abstract_inverted_index.substitution | 140 |
| abstract_inverted_index.self-renewal, | 55 |
| abstract_inverted_index.self-renewal. | 16 |
| abstract_inverted_index.transcription | 4, 205 |
| abstract_inverted_index.understanding | 198 |
| abstract_inverted_index.LIF-independent | 54, 192 |
| abstract_inverted_index.differentiation. | 228 |
| abstract_inverted_index.homodimerization, | 95 |
| abstract_inverted_index.heterodimerization | 97 |
| cited_by_percentile_year.max | 98 |
| cited_by_percentile_year.min | 90 |
| corresponding_author_ids | https://openalex.org/A5085359324, https://openalex.org/A5032204999 |
| countries_distinct_count | 3 |
| institutions_distinct_count | 7 |
| corresponding_institution_ids | https://openalex.org/I4210108209, https://openalex.org/I98677209 |
| citation_normalized_percentile.value | 0.80762684 |
| citation_normalized_percentile.is_in_top_1_percent | False |
| citation_normalized_percentile.is_in_top_10_percent | False |