The DOI matches its Crossref record.
A DNA-Unwinding Protein Isolated from Escherichia coli: Its Interaction with DNA and with DNA Polymerases
Open accessAbstract
A DNA-unwinding protein has been purified to homogeneity from E. coli . This protein has a molecular weight of about 22,000, as judged by its electrophoretic mobility on polyacrylamide gels containing sodium dodecylsulfate, and it appears to be present in about 800 copies per log-phase cell. It binds tightly and cooperatively to single-stranded DNA, and much less tightly, if at all, to RNA or double-stranded DNA. Like the T4 gene-32 protein characterized previously, the E. coli DNA-unwinding protein depresses the melting temperature of double-stranded DNAs, with regions rich in A-T base-pairs being preferentially melted. The E. coli protein strongly stimulates in vitro DNA synthesis by E. coli DNA polymerase II on appropriate templates; however, no stimulation is found with purified polymerases I or III of E. coli , or with T4 DNA polymerase. In contrast, gene-32 protein stimulates only the T4 DNA polymerase in a parallel assay.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cited by
Cook, P. R., & Brazell, I. A. (1975) · Journal of Cell Science · doi:10.1242/jcs.19.2.261 · Cited by 486
Regulation of Bacterial RecA Protein Function
Cox, M. M. (2007) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230701260258 · Cited by 417
McGhee, J. D. (1976) · Biopolymers · doi:10.1002/bip.1976.360150710 · Cited by 309
McEntee, K., Weinstock, G. M., & Lehman, I. R. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.2.857 · Cited by 232
Metadata
- Authors
- Sigal, N., Delius, H., Kornberg, T., Gefter, M. L., & Alberts, B.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1972-12
- Volume
- 69
- Issue
- 12
- Pages
- 3537-3541
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2056082657
- Cited by
- 358
- References
- 0
- FWCI
- 20.02
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: A DNA-Unwinding Protein Isolated from Escherichia coli: Its Interaction with DNA and with DNA Polymerases. https://app.cochat.ai/papers/10.1073/pnas.69.12.3537
- The paper
- Sigal, N., Delius, H., Kornberg, T., Gefter, M. L., & Alberts, B. (1972). A DNA-Unwinding Protein Isolated from Escherichia coli: Its Interaction with DNA and with DNA Polymerases. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.69.12.3537
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
