Karolin Luger | |
---|---|
Citizenship | Austria, USA |
Alma mater | University of Basel |
Known for | Discovering the three-dimensional structure of chromatin |
Awards | Vorarlberg Science Prize, Searle Scholar Award, World Laureates Association Prize |
Scientific career | |
Fields | biochemistry, biophysics |
Institutions | Swiss Federal Institute of Technology, Colorado State University, University of Colorado, Howard Hughes Medical Institute |
Website | www |
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 Distinguished Professor at the University of Colorado Boulder in the Biochemistry Department.
Luger was born the youngest child after several brothers. Though not interested in mathematics, electronics, or physics, as her brothers were, she became fascinated with biology. She has stated that she chose a career in science during middle school, when she realized that "not everything was 'known' yet". [1] As a young woman in Austria, Luger attended a gymnasium where she specialized in foreign languages. [1]
Luger is married and has one daughter. [1]
Luger earned a Bachelor of Science in microbiology and a Master of Science in biochemistry from the University of Innsbruck. [2] She completed her Ph.D in biochemistry and biophysics at the University of Basel. [2] [3]
In 1997, as a postdoc with Timothy J Richmond, Luger was first author on the paper that described the first structure determined for the nucleosome. The structure was discovered by X-ray crystallography. [2] [4] She also proposed that histone-DNA bonds are weaker at points where less of the histone contacts the DNA, which was confirmed by Michelle Wang in a 2009 paper. [5] After several years at the Swiss Federal Institute of Technology, Luger was hired by Colorado State University in 1999. [6] [7] Her work there includes extensive further research on the nucleosome's three-dimensional structure. [6] The nucleosome, a building block of the chromatin genetic material that makes up chromosomes, consists of DNA wrapped around a disk of proteins. In 2005, Luger and Kenneth Kaye used X-ray crystallography to determine the mechanism that the virus causing Kaposi's sarcoma, a cancer that affects subdermal connective tissue, uses to spread. The virus attaches to chromatin and inserts its genetic material, which is then copied along with the cell's DNA. Luger and Kaye thus showed that a virus can attach to chromatin as a "docking platform". [8]
Since 2010, Luger has done significant studies of histones, researching the connection between their chaperone proteins and acetylation, as well as variant structures. [7] [9] Histones are important in the process of gene expression, and their positioning as determined by chaperone proteins is essential to that role. The chaperones also can change the conformation of the nucleosome as a whole. [2] Modifications to histones, including acetylation, methylation, and phosphorylation, are important because of their role in activating and deactivating genes. [5] In 2008, Luger published a study that showed that physical changes to the nucleosome do not occur when DNA is methylated. [10] Luger's research as of 2012 also comprises several other areas of study with chromatin, including the processes of DNA replication, transcription, recombination, and repair in chromatin. [9] She and her research group have also developed various assays for examining chromatin structure, to augment traditional X-ray crystallography. [9] Another related research interest for Luger's research group is the genetic cause of Rett syndrome, the gene MECP2. The gene codes for a protein that binds to methyl groups on chromatin, altering its conformation. [5]
Luger has received many honors throughout her career. She was the recipient of the Searle Scholar Award in 1999, her first year as a professor at Colorado State University. In 2003, she was named a Monfort Professor and awarded $75,000 a year for two years in research funds by the university. [6] Two years later, Luger was appointed as an investigator at the Howard Hughes Medical Institute. [2] [7] In 2007 she received the State Science Prize of Vorarlberg Austria. From 2008 to 2012, Luger sat on the National Institute of General Medical Sciences' advisory board. [11]
She has also received several prestigious grants throughout her career, including a 5-year award from the National Institute of Health and a $1.2 million grant from the W. M. Keck Foundation. [6]
In 2007, Luger was named CSU University Distinguished Professor [12]
In 2012, Luger was chosen to be the National Lecturer for the Biophysical Society's 2013 meeting. [11]
In 2014, Luger was named 2014 Fellow Of The Biophysical Society [13]
In 2017, Luger has been selected to the American Academy of Arts and Sciences. [14]
In 2018, Luger was elected to the National Academy of Sciences. [15]
In 2023, Luger was named a CU distinguished Professor [16]
In 2023, Luger, Rhodes and Richmond were awarded the World Laureates Association Prize [17] for elucidating the structure of the nucleosome at the atomic level
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.
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.
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.
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