The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Histone Acetyltransferase Activity Is Conserved between Yeast and Human GCN5 and Is Required for Complementation of Growth and Transcriptional Activation
Open accessAbstract
Yeast and human ADA2 and GCN5 (y- and hADA2 and y- and hGCN5, respectively) have been shown to potentiate transcription in vivo and may function as adaptors to bridge physical interactions between DNA-bound activators and the basal transcriptional machinery. Recently it was shown that yGCN5 is a histone acetyltransferase (HAT), suggesting a link between enzymatic modification of nucleosomes and transcriptional activation. In this report, we demonstrate that hGCN5 is also an HAT and has the same substrate specificity as yGCN5. Since hGCN5 does not complement functional defects caused by deletion of yGCN5, we constructed a series of hGCN5-yGCN5 chimeras to identify human regions capable of activity in yeast. Interestingly, only the putative HAT domain of hGCN5, when fused to the remainder of yGCN5, complemented gcn5- cells for growth and transcriptional activation. Moreover, an amino acid substitution mutation within the HAT domain reduced both HAT activity in vitro and transcription in vivo. These findings directly link enzymatic histone acetylation and transcriptional activation and show evolutionary conservation of this potentially crucial pathway in gene regulation.
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
Cites
Phosphorylated CREB binds specifically to the nuclear protein CBP
Chrivia, J. C., Kwok, R. P. S., Lamb, N., Hagiwara, M., Montminy, M. R., & Goodman, R. H. (1993) · Nature · doi:10.1038/365855a0 · Cited by 2,052
Nuclear protein CBP is a coactivator for the transcription factor CREB
Kwok, R. P. S., Lundblad, J. R., Chrivia, J. C., Richards, J. P., Bächinger, H. P., Brennan, R. G., Roberts, S. G. E., Green, M. R., & Goodman, R. H. (1994) · Nature · doi:10.1038/370223a0 · Cited by 1,443
Berger, S. L., Piña, B., Silverman, N., Marcus, G. A., Agapite, J., Regier, J. L., Triezenberg, S. J., & Guarente, L. (1992) · Cell · doi:10.1016/0092-8674(92)90100-q · Cited by 435
Self-citationMarcus, G. A., Silverman, N., Berger, S. L., Horiuchi, J., & Guarente, L. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06806.x · Cited by 276
Cited by
Grant, P. A., Duggan, L., Côté, J., Roberts, S. M., Brownell, J. E., Candau, R., Ohba, R., Owen-Hughes, T., Allis, C. D., Winston, F., et al. (1997) · Genes & Development · doi:10.1101/gad.11.13.1640 · Cited by 1,085
Self-citationGlass, C. K., Rose, D. W., & Rosenfeld, M. G. (1997) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(97)80066-x · Cited by 698
Transcriptional coactivator complexes.
Näär, A. M., Lemon, B. D., & Tjian, R. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.475 · Cited by 571
The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc
McMahon, S. B., Wood, M. A., & Cole, M. D. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.2.556-562.2000 · Cited by 494
Maternal programming of steroid receptor expression and phenotype through DNA methylation in the rat
Szyf, M., Weaver, I. C. G., Champagne, F. A., Diorio, J., & Meaney, M. J. (2005) · Frontiers in Neuroendocrinology · doi:10.1016/j.yfrne.2005.10.002 · Cited by 348
Metadata
- Authors
- Wang, L., Mizzen, C., Ying, C., Candau, R., Barlev, N., Brownell, J., Allis, C. D., & Berger, S. L.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 1997-01-01
- Volume
- 17
- Issue
- 1
- Pages
- 519-527
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- OpenAlex
- W2170799477
- Cited by
- 168
- References
- 4
- FWCI
- 6.75
- 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: Histone Acetyltransferase Activity Is Conserved between Yeast and Human GCN5 and Is Required for Complementation of Growth and Transcriptional Activation. https://app.cochat.ai/papers/10.1128/mcb.17.1.519
- The paper
- Wang, L., Mizzen, C., Ying, C., Candau, R., Barlev, N., Brownell, J., Allis, C. D., & Berger, S. L. (1997). Histone Acetyltransferase Activity Is Conserved between Yeast and Human GCN5 and Is Required for Complementation of Growth and Transcriptional Activation. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.17.1.519
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.