Timothy J. Richmond

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Timothy John Richmond (born October 9, 1948, in Corvallis) is a Swiss/American molecular biologist, biochemist, and biophysicist.

He graduated in 1970 with a bachelor's degree [1] in biochemistry from Purdue University, where his teachers included Larry G. Butler (died 1997) and Michael G. Rossmann. Richmond graduated in 1975 from Yale University's department of molecular biophysics and biochemistry with a dissertation on protein-DNA interaction under the supervision of Frederic M. Richards and Thomas A. Steitz. Richmond was a postdoc at Yale University from 1975 to 1978 under the supervision of Frederic M. Richards and from 1978 to 1980 at the MRC Laboratory of Molecular Biology under the supervision of Sir Aaron Klug studying the nucleosome (which is the fundamental subunit of chromatin). [2] Richmond was from 1980 to 1987 a tenured staff scientist at the MRC Laboratory of Molecular Biology [1] and in 1987 was appointed "Professor of X-ray Crystallography of Biological Macromolecules" [2] at ETH Zurich's Institute for Molecular Biology and Biophysics. [1] At ETH Zurich he became in 2005 vice-chair of the biology department. [2]

Richmond’s work provides a basis for integrating decades of biochemical, physical, and genetic studies of chromatin. His focus has been to establish the atomic structures of large macromolecular assemblies, particularly those involved in protein-DNA complexes and to relate these structures to the biological processes of chromatin assembly and transcription regulation. [3]

The interests of Prof. Richmond in teaching and research are primarily devoted to the recognition and assembly of biological macromolecular complexes. X-ray crystallography, cryo-electron microscopy and other biophysical and biochemical techniques are employed by his laboratory. The focus of his research is on the organization of DNA in chromosomes and the regulation of gene expression in higher organisms. His laboratory has elucidated the structures of the nucleosome core particle and various transcription factor complexes. Their work on the nucleosome core particle, the fundamental repeating unit of chromatin, resulted ultimately in its atomic description at 1.9 å resolution. They have since determined the organization of nucleosomes in the chromatin fiber. [4]

He was the postdoctoral supervisor of Karolin Luger. [5]

Richmond was elected in 1994 a fellow of the American Association for the Advancement of Science (AAAS). [6] He was elected a member in 1995 of the European Molecular Biology Organization (EMBO), [7] in 2000 of the Academia Europaea, [1] in 2004 of the German National Academy of Sciences Leopoldina, [2] and in 2007 of the U.S. National Academy of Sciences. [8] In 2001 he was awarded an honorary doctor of science degree by Purdue University. [9] His prizes or awards include the Louis-Jeantet Prize for Medicine in 2002 [10] and the Marcel Benoist Prize in 2006. [11] In 2023, Timothy J. Richmond, Daniela Rhodes and Karolin Luger were awarded the WLA Prize in Life Science or Medicine "for elucidating the structure of the nucleosome at the atomic level, providing the basis for understanding chromatin, gene regulation, and epigenetics." [12]

Selected publications

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">Histone</span> Family proteins package and order the DNA into structural units called nucleosomes.

In biology, histones are highly basic proteins abundant in lysine and arginine residues that are found in eukaryotic cell nuclei and in most Archaeal phyla. They act as spools around which DNA winds to create structural units called nucleosomes. Nucleosomes in turn are wrapped into 30-nanometer fibers that form tightly packed chromatin. Histones prevent DNA from becoming tangled and protect it from DNA damage. In addition, histones play important roles in gene regulation and DNA replication. Without histones, unwound DNA in chromosomes would be very long. For example, each human cell has about 1.8 meters of DNA if completely stretched out; however, when wound about histones, this length is reduced to about 90 micrometers (0.09 mm) of 30 nm diameter chromatin fibers.

<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.

<span class="mw-page-title-main">Euchromatin</span> Lightly packed form of chromatin that is enriched in genes

Euchromatin is a lightly packed form of chromatin that is enriched in genes, and is often under active transcription. Euchromatin stands in contrast to heterochromatin, which is tightly packed and less accessible for transcription. 92% of the human genome is euchromatic.

<span class="mw-page-title-main">Histone octamer</span> 8-protein complex forming the core of nucleosomes

In molecular biology, a histone octamer is the eight-protein complex found at the center of a nucleosome core particle. It consists of two copies of each of the four core histone proteins. The octamer assembles when a tetramer, containing two copies of H3 and two of H4, complexes with two H2A/H2B dimers. Each histone has both an N-terminal tail and a C-terminal histone-fold. Each of these key components interacts with DNA in its own way through a series of weak interactions, including hydrogen bonds and salt bridges. These interactions keep the DNA and the histone octamer loosely associated, and ultimately allow the two to re-position or to separate entirely.

<span class="mw-page-title-main">Histone H1</span> Components of chromatin in eukaryotic cells

Histone H1 is one of the five main histone protein families which are components of chromatin in eukaryotic cells. Though highly conserved, it is nevertheless the most variable histone in sequence across species.

<span class="mw-page-title-main">Histone H2A</span> One of the five main histone proteins

Histone H2A is one of the five main histone proteins involved in the structure of chromatin in eukaryotic cells.

<span class="mw-page-title-main">Solenoid (DNA)</span>

The solenoid structure of chromatin is a model for the structure of the 30 nm fibre. It is a secondary chromatin structure which helps to package eukaryotic DNA into the nucleus.

Chromatin remodeling is the dynamic modification of chromatin architecture to allow access of condensed genomic DNA to the regulatory transcription machinery proteins, and thereby control gene expression. Such remodeling is principally carried out by 1) covalent histone modifications by specific enzymes, e.g., histone acetyltransferases (HATs), deacetylases, methyltransferases, and kinases, and 2) ATP-dependent chromatin remodeling complexes which either move, eject or restructure nucleosomes. Besides actively regulating gene expression, dynamic remodeling of chromatin imparts an epigenetic regulatory role in several key biological processes, egg cells DNA replication and repair; apoptosis; chromosome segregation as well as development and pluripotency. Aberrations in chromatin remodeling proteins are found to be associated with human diseases, including cancer. Targeting chromatin remodeling pathways is currently evolving as a major therapeutic strategy in the treatment of several cancers.

FACT is a heterodimeric protein complex that affects eukaryotic RNA polymerase II transcription elongation both in vitro and in vivo. It was discovered in 1998 as a factor purified from human cells that was essential for productive, in vitro Pol II transcription on a chromatinized DNA template.

<span class="mw-page-title-main">Daniela Rhodes</span> British structural and molecular biologist

Daniela Bargellini Rhodes FRS is an Italian structural and molecular biologist. She was a senior scientist at the Laboratory of Molecular Biology in Cambridge, England, where she worked, and later studied for her PhD under the supervision of Nobel laureate Aaron Klug. Continuing her work under the tutelage of Aaron Klug at Cambridge, she was appointed group leader in 1983, obtained tenure in 1987 and was promoted to senior scientist in 1994. Subsequently, she served as director of studies between 2003 and 2006. She has also been visiting professor at both "La Sapienza" in Rome, Italy and the Rockefeller University in NY, USA.

<span class="mw-page-title-main">H2AFB3</span> Protein-coding gene in the species Homo sapiens

H2A histone family, member B3 is a protein that in humans is encoded by the H2AFB3 gene.

<span class="mw-page-title-main">Karolin Luger</span> Austrian-American biochemist and biophysicist

Karolin Luger is an Austrian-American biochemist and biophysicist known for her work with nucleosomes and discovery of the three-dimensional structure of chromatin. She is a University Distinguished Professor at Colorado State University in Fort Collins and works with the University of Colorado School of Medicine's Department of Biochemistry and Molecular Genetics.

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.

<span class="mw-page-title-main">Nuclear organization</span> Spatial distribution of chromatin within a cell nucleus

Nuclear organization refers to the spatial distribution of chromatin within a cell nucleus. There are many different levels and scales of nuclear organisation. Chromatin is a higher order structure of DNA.

H3K27me3 is an epigenetic modification to the DNA packaging protein Histone H3. It is a mark that indicates the tri-methylation of lysine 27 on histone H3 protein.

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.

H3K56ac is an epigenetic modification to the DNA packaging protein Histone H3. It is a mark that indicates the acetylation at the 56th 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.

H3T45P is an epigenetic modification to the DNA packaging protein histone H3. It is a mark that indicates the phosphorylation the 45th threonine residue of the histone H3 protein.

References

  1. 1 2 3 4 "Timothy J. Richmond (membership number 2024)". Academia Europaea.
  2. 1 2 3 4 "Neue Mitglieder der Leopoldina 2004" (PDF). Deutsche Akademie der Naturforscher Leopoldina. p. 70.
  3. ↑ "2010 Bios". Yale Graduate School of Arts and Sciences.
  4. ↑ "Richmond, Timothy J., Prof. Dr". ETH Zürich.
  5. ↑ "Timothy J. Richmond, Ph.D." Chemistry Tree (academictree.org).
  6. ↑ "Historic Fellows". American Association for the Advancement of Science (aaas.org).
  7. ↑ "EMBO Member Timothy J. Richmond". EMBO.
  8. ↑ "Member Directory: Timothy J. Richmond". National Academy of Sciences.
  9. ↑ "Timothy Richmond". Purdue to award 15 honorary doctorates, Purdue News. April 2001.
  10. ↑ "Professor Timothy J. Richmond, Winner of the 2002 Louis-Jeantet Prize for medicine". Fondation Louis-Jeantet. October 2017.
  11. ↑ "Laureates". Marcel Benoist Foundation.
  12. ↑ Laureates of the 2023 WLA Prize Announced, The WLA Prize
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