Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules
Abstract
The structure of an Oct-1 POU domain-octamer DNA complex has been solved at 3.0 A resolution. The POU-specific domain contacts the 5' half of this site (ATGCAAAT), and as predicted from nuclear magnetic resonance studies, the structure, docking, and contacts are remarkably similar to those of the lambda and 434 repressors. The POU homeodomain contacts the 3' half of this site (ATGCAAAT), and the docking is similar to that of the engrailed, MAT alpha 2, and Antennapedia homeodomains. The linker region is not visible and there are no protein-protein contacts between the domains, but overlapping phosphate contacts near the center of the octamer site may favor cooperative binding. This novel arrangement raises important questions about cooperativity in protein-DNA recognition.
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The POU domain linker flexibly connects the POU homeo- and POU-specific domains and appears unstructured in the Oct-1-DNA co-crystal structure.
“This linker was chosen because it flexibly connects the POU homeo-and POUspecific domains (Herr and Cleary, 1995), and appears unstructured in the Oct-1-DNA co-crystal structure (Klemm et al., 1994).”
From Assembly requirements of PU.1–Pip (IRF‐4) activator complexes: inhibiting function in vivo using fused dimers (1999) · cites this paper as Klemm et al., 1994
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- Authors
- Klemm, J. D., Rould, M. A., Aurora, R., Herr, W., & Pabo, C. O.
- Affiliations
- Massachusetts Institute of Technology (US)
- Howard Hughes Medical Institute (US)
- Cold Spring Harbor Laboratory (US)
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1994-04
- Volume
- 77
- Issue
- 1
- Pages
- 21-32
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2004689349
- Cited by
- 506
- References
- 58
- Citations by year
- 2026: 3 · 2025: 8 · 2024: 7 · 2023: 1 · 2022: 3 · 2021: 5 · 2020: 7 · 2019: 3 · 2018: 7 · 2017: 9 · 2016: 9 · 2015: 5 · 2014: 8 · 2013: 11 · 2012: 7
- FWCI
- 19.49
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Cold Spring Harbor Laboratory Institutional Repository (Cold Spring Harbor Laboratory) (acceptedVersion)
- Funders
- National Institutes of Health (5r01gm031471-16)
- U.S. Public Health Service (5-T32-6MO7287-18)
- National Cancer Institute (CA13106, P01CA013106)
- National Institute of General Medical Sciences (GM-31471)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- Oct-1, POU domain, protein-DNA recognition, homeodomain, cooperative DNA binding, transcription factor-DNA complex
- MeSH terms
- Amino Acid Sequence, Base Sequence, Binding Sites, Deoxyribonucleoproteins, DNA, DNA-Binding Proteins, Molecular Sequence Data, Nucleic Acid Conformation, Repressor Proteins, Transcription Factors, Protein Structure, Tertiary, Crystallography, X-Ray, Octamer Transcription Factor-1, Host Cell Factor C1
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