Carl Wu

Last updated
Carl Wu
CitizenshipAmerican
Education
Awards National Academy of Medicine (2010)

National Academy of Sciences (2006)
American Academy of Arts and Sciences
European Molecular Biology Organization

Academia Sinica

Contents

Scientific career
Fields Molecular Biology, Genetics, Biochemistry
Institutions Johns Hopkins University (Since 2016)
Howard Hughes Medical Institute (2012-2016)
National Cancer Institute (1982-2012)

Carl Wu is a Chinese-American scientist, and a Bloomberg Distinguished Professor of biology, molecular biology and genetics at Johns Hopkins University. [1] He is active in the fields of chromatin and gene expression.

Early life and education

Carl Wu was born in Hong Kong. Wu attended St. Joseph's High School in Hong Kong and won a scholarship to attend Saint Mary's College of California. He began his research in chromatin biology while pursuing his doctorate at Harvard University, under Sarah Elgin. Subsequently, Wu completed his post-doc as a Junior fellow of the Harvard Society of Fellows under Nobel laureate Walter Gilbert, where he provided the first evidence for DNase hypersensitive sites at cellular gene promoters. [2]

Career

National Cancer Institute and HHMI

In 1982, Wu joined the National Cancer Institute within the National Institutes of Health. Here he began investigating the biochemical mechanism of chromatin remodeling. In 1994, his group discovered that enzymatic activity was necessary for creating accessible DNA sites on chromatin. The following year his lab purified and characterized the responsible chromatin remodeling enzyme called NURF. This work was recognized by Nature as a breakthrough discovery in the field of gene expression. Wu went on to become the chief of the Laboratory for Molecular Cell Biology at the cancer institute; then chief of the Laboratory of Biochemistry and Molecular Biology. [3]

In 2012, Wu joined Janelia Research Campus of the Howard Hughes Medical Institute as a Senior Fellow of the Transcription Imaging Consortium.[ citation needed ]

Johns Hopkins University

In 2016, Wu joined the Johns Hopkins University as the 23rd Bloomberg Distinguished Professor. His appointment bridges the Department of Biology in JHU's Zanvyl Krieger School of Arts and Sciences and the Department of Molecular Biology and Genetics in the School of Medicine. Through this interdisciplinary appointment, Wu combined his research efforts in biochemistry and live cell imaging into a single unified effort. [4]

Awards

Wu was elected as a member of the National Academy of Sciences in 2006 and the National Academy of Medicine in 2010. [5] [6] He is also a Member of Academia Sinica [7] and the European Molecular Biology Organization, and a fellow of the American Academy of Arts and Sciences.

Publications

Wu has more than 30,000 citations in Google Scholar and an h-index of 83. [8]

Selected articles

Related Research Articles

Chromatin is a complex of DNA and protein found in eukaryotic cells. The primary function is to package long DNA molecules into more compact, denser structures. This prevents the strands from becoming tangled and also plays important roles in reinforcing the DNA during cell division, preventing DNA damage, and regulating gene expression and DNA replication. During mitosis and meiosis, chromatin facilitates proper segregation of the chromosomes in anaphase; the characteristic shapes of chromosomes visible during this stage are the result of DNA being coiled into highly condensed chromatin.

<span class="mw-page-title-main">Nucleosome</span> Basic structural unit of DNA packaging in eukaryotes

A nucleosome is the basic structural unit of DNA packaging in eukaryotes. The structure of a nucleosome consists of a segment of DNA wound around eight histone proteins and resembles thread wrapped around a spool. The nucleosome is the fundamental subunit of chromatin. Each nucleosome is composed of a little less than two turns of DNA wrapped around a set of eight proteins called histones, which are known as a histone octamer. Each histone octamer is composed of two copies each of the histone proteins H2A, H2B, H3, and H4.

Epigenomics is the study of the complete set of epigenetic modifications on the genetic material of a cell, known as the epigenome. The field is analogous to genomics and proteomics, which are the study of the genome and proteome of a cell. Epigenetic modifications are reversible modifications on a cell's DNA or histones that affect gene expression without altering the DNA sequence. Epigenomic maintenance is a continuous process and plays an important role in stability of eukaryotic genomes by taking part in crucial biological mechanisms like DNA repair. Plant flavones are said to be inhibiting epigenomic marks that cause cancers. Two of the most characterized epigenetic modifications are DNA methylation and histone modification. Epigenetic modifications play an important role in gene expression and regulation, and are involved in numerous cellular processes such as in differentiation/development and tumorigenesis. The study of epigenetics on a global level has been made possible only recently through the adaptation of genomic high-throughput assays.

H3K4me3 is an epigenetic modification to the DNA packaging protein Histone H3 that indicates tri-methylation at the 4th lysine residue of the histone H3 protein and is often involved in the regulation of gene expression. The name denotes the addition of three methyl groups (trimethylation) to the lysine 4 on the histone H3 protein.

H3K27ac is an epigenetic modification to the DNA packaging protein histone H3. It is a mark that indicates acetylation of the lysine residue at N-terminal position 27 of the histone H3 protein.

Nucleosome Remodeling Factor (NURF) is an ATP-dependent chromatin remodeling complex first discovered in Drosophila melanogaster that catalyzes nucleosome sliding in order to regulate gene transcription. It contains an ISWI ATPase, making it part of the ISWI family of chromatin remodeling complexes. NURF is highly conserved among eukaryotes and is involved in transcriptional regulation of developmental genes.

H3K9me3 is an epigenetic modification to the DNA packaging protein Histone H3. It is a mark that indicates the tri-methylation at the 9th lysine residue of the histone H3 protein and is often associated with heterochromatin.

H3K4me1 is an epigenetic modification to the DNA packaging protein Histone H3. It is a mark that indicates the mono-methylation at the 4th lysine residue of the histone H3 protein and often associated with gene enhancers.

H4K16ac is an epigenetic modification to the DNA packaging protein Histone H4. It is a mark that indicates the acetylation at the 16th lysine residue of the histone H4 protein.

H4K5ac is an epigenetic modification to the DNA packaging protein histone H4. It is a mark that indicates the acetylation at the 5th lysine residue of the histone H4 protein. H4K5 is the closest lysine residue to the N-terminal tail of histone H4. It is enriched at the transcription start site (TSS) and along gene bodies. Acetylation of histone H4K5 and H4K12ac is enriched at centromeres.

H4K8ac, representing an epigenetic modification to the DNA packaging protein histone H4, is a mark indicating the acetylation at the 8th lysine residue of the histone H4 protein. It has been implicated in the prevalence of malaria.

H4K12ac is an epigenetic modification to the DNA packaging protein histone H4. It is a mark that indicates the acetylation at the 12th lysine residue of the histone H4 protein. H4K12ac is involved in learning and memory. It is possible that restoring this modification could reduce age-related decline in memory.

H4K91ac is an epigenetic modification to the DNA packaging protein histone H4. It is a mark that indicates the acetylation at the 91st lysine residue of the histone H4 protein. No known diseases are attributed to this mark but it might be implicated in melanoma.

H3K23ac is an epigenetic modification to the DNA packaging protein Histone H3. It is a mark that indicates the acetylation at the 23rd lysine residue of the histone H3 protein.

H3K14ac is an epigenetic modification to the DNA packaging protein Histone H3. It is a mark that indicates the acetylation at the 14th lysine residue of the histone H3 protein.

<span class="mw-page-title-main">MNase-seq</span> Sk kasid Youtuber

MNase-seq, short for micrococcal nuclease digestion with deep sequencing, is a molecular biological technique that was first pioneered in 2006 to measure nucleosome occupancy in the C. elegans genome, and was subsequently applied to the human genome in 2008. Though, the term ‘MNase-seq’ had not been coined until a year later, in 2009. Briefly, this technique relies on the use of the non-specific endo-exonuclease micrococcal nuclease, an enzyme derived from the bacteria Staphylococcus aureus, to bind and cleave protein-unbound regions of DNA on chromatin. DNA bound to histones or other chromatin-bound proteins may remain undigested. The uncut DNA is then purified from the proteins and sequenced through one or more of the various Next-Generation sequencing methods.

H3K36me is an epigenetic modification to the DNA packaging protein Histone H3, specifically, the mono-methylation at the 36th lysine residue of the histone H3 protein.

H3R17me2 is an epigenetic modification to the DNA packaging protein histone H3. It is a mark that indicates the di-methylation at the 17th arginine residue of the histone H3 protein. In epigenetics, arginine methylation of histones H3 and H4 is associated with a more accessible chromatin structure and thus higher levels of transcription. The existence of arginine demethylases that could reverse arginine methylation is controversial.

H3R8me2 is an epigenetic modification to the DNA packaging protein histone H3. It is a mark that indicates the di-methylation at the 8th arginine residue of the histone H3 protein. In epigenetics, arginine methylation of histones H3 and H4 is associated with a more accessible chromatin structure and thus higher levels of transcription. The existence of arginine demethylases that could reverse arginine methylation is controversial.

H4R3me2 is an epigenetic modification to the DNA packaging protein histone H4. It is a mark that indicates the di-methylation at the 3rd arginine residue of the histone H4 protein. In epigenetics, arginine methylation of histones H3 and H4 is associated with a more accessible chromatin structure and thus higher levels of transcription. The existence of arginine demethylases that could reverse arginine methylation is controversial.

References

  1. ↑ "Carl Wu | Department of Biology". Department of Biology. Retrieved 2018-07-16.
  2. ↑ "The 5′ ends of Drosophila heat shock genes in chromatin are hypersensitive to DNase I". Nature. 1980-08-28. Retrieved 2018-12-06.
  3. ↑ "Carl Wu, Ph.D." Center for Cancer Research. 2014-08-12. Retrieved 2018-07-16.
  4. ↑ "Renowned scientist Carl Wu named Bloomberg Distinguished Professor at Johns Hopkins". The Hub. 2016-08-03. Retrieved 2018-07-16.
  5. ↑ "Carl Wu". www.nasonline.org. Retrieved 2018-07-16.
  6. ↑ "Five NIH leaders elected to the Institute of Medicine". National Institutes of Health (NIH). 2015-09-01. Retrieved 2018-07-16.
  7. ↑ "Carl Wu". Academia Sinica. Retrieved 16 March 2022.
  8. ↑ "Carl Wu".
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