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Dr. Christiane Menzfeld
Dr. Christiane Menzfeld
Public Relations
Phone:+49 89 8578-2824
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MPI of Biochemistry, Am Klopferspitz 18, 82152 Martinsried

www.biochem.mpg.de

Prof. Dr. Franz-Ulrich Hartl
Prof. Dr. Franz-Ulrich Hartl
Director
Phone:+49 89 8578-2244

MPI of Biochemistry, Am Klopferspitz 18, 82152 Martinsried

www.biochem.mpg.de/hartl

Cellular Biochemistry

Cellular Biochemistry

It is a Matter of Form

The chaperonin GroEL/GroES helps other proteins to receive the correct form. Zoom Image
The chaperonin GroEL/GroES helps other proteins to receive the correct form.

Proteins acquire their correct conformation and can function properly only through folding. Misfolding can lead to diseases such as Alzheimer’s or Parkinson’s disease. But who ensures that nothing goes wrong? Franz-Ulrich Hartl and his team are interested both in the underlying mechanisms as well as the structure of the involved molecules.

Proteins are molecules composed of long amino acid chains with a very complex three-dimensional structure. Hence, there are millions of possible ways to build these molecules – but only one way is correct and guarantees that the protein can fulfill its task. Proteins serving as “molecular chaperones” ensure that other proteins maintain their proper conformation. With their help, only the correct parts of the newly produced proteins come together to build a proper three-dimensional structure.

Chaperones at work

A special subgroup of the chaperones are the chaperonins. They form hollow cylinder-shaped complexes with a lid that look like a cage and provide a protected space for other proteins to fold. As shown for the chaperonin GroEL/GroES, these nano-cages not only shield proteins during folding, they also actively support the folding process. They may even repair misfolded proteins.

When folding goes awry

Misfolded proteins easily clump together to form insoluble aggregates which are then deposited in the cell and cause damage. Deposits of such protein aggregates are typical for neurodegenerative diseases such as Alzheimer’s, Parkinson’s or Huntington’s disease. Molecular chaperones can prevent this. Elucidating the structural requirements and mechanisms of chaperone activity may thus contribute to developing new drugs for the treatment of severe neurodegenerative diseases.

Press Releases from the Hartl Department

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F.-Ulrich Hartl receives Breakthrough Prize 2020

September 05, 2019
The biochemist Hartl and the geneticist Horwich are honored with the world’s highest science prize for their groundbreaking discovery of the protein folding, assistans, chaperones. [more]
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The nucleolus – a known organelle with new tasks

July 12, 2019
The nucleolus is a well-known cellular structure that is easily visible under a light microscope. This nuclear structure is known as the site of ribosome production. In a recent study, researchers at the Max Planck Institute of Biochemistry in Martinsried, Germany, have shown that the nucleolus is also a site of quality control for proteins. When cells are stressed, proteins tend to misfold and to aggregate. To prevent proteins from clumping, some are temporarily stored in the nucleolus. The special biophysical conditions found in this organelle prevent harmful protein aggregation. The results of this study have now been published in the journal Science. [more]
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Dr. Paul Janssen Award for Biomedical Research for F.-Ulrich Hartl

June 03, 2019

F.-Ulrich Hartl, Director at the Max Planck Institute of Biochemistry, and Arthur Horwich of Yale School of Medicine and Howard Hughes Medical Institute were named winners of the 2019 Dr. Paul Janssen Award for Biomedical Research. Selected by an independent committee of world-renowned scientists, Hartl and Horwich won for their revolutionary insights into chaperone-mediated protein folding. Hartl expresses his delight to have been selected as one of the winners of the Dr. Paul Janssen Award. “This is a fantastic honor and recognition of the work of my laboratory”, he says. The award includes a $200,000 prize and will be presented at ceremonies in the USA and Belgium in September.

[more]
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Paul Ehrlich- and Ludwig Darmstaedter-Prize for F.-Ulrich Hartl

January 16, 2019

F.-Ulrich Hartl, Director at the Max Planck Institute of Biochemistry in Martinsried near Munich, is awarded the Paul Ehrlich- and Ludwig Darmstaedter-Prize 2019 together with Arthur L. Horwich.  of Yale School of Medicine/HHMI.The biochemist Hartl and the geneticist Horwich are honored for their pioneering work in the field of cellular protein chemistry. Their collaboration helped unravel the molecular machinery that assists protein folding. The prize will be awarded on March 14 in the St. Paul‘s Church in Frankfurt and is endowed with 120,000 EUR.

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F.-Ulrich Hartl inducted into Hall of Fame of German Research

November 02, 2018

F.-Ulrich Hartl, director at the Max Planck Institute of Biochemistry in Martinsried, was inducted into the Hall of Fame of German Research. The award, which was introduced by the Manager Magazin in 2009, honors Hartl as a pioneer in the field of cellular biochemistry. Together with colleagues in the USA, Hartl demonstrated that newly produced proteins do not fold spontaneously but require the assistance by folding helpers, so called chaperones. This finding refuted the central dogma that proteins in cells can fold spontaneously, just as they do in the test tube. Hartl’s research shows that misfolded proteins contribute to neurodegenerative diseases like Alzheimer’s and Parkinson’s disease and are associated with malfunction of chaperones.

 

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The “TRiC” to folding actin

August 09, 2018

Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.

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E.B. Wilson Medal for F.-Ulrich Hartl

December 05, 2017
F.-Ulrich Hartl, director at the Max Planck Institute of Biochemistry in Martinsried, is awarded the E.B. Wilson Medal this year together with Arthur L. Horwich of Yale School of Medicine/HHMI. The award represents the highest honor of the American Society of Cell Biology (ASCB). The biochemist Hartl and the geneticist Horwich are pioneers in the field of cellular protein chemistry. Their collaboration helped unravel the molecular machinery that assists protein folding. Hartl and Horwich challenged the widely held notion put forth by Nobel Prize winner Christian Anfinsen that proteins fold spontaneously in cells, just as they do in test tubes. The prize will be awarded on December 5 on the ASCB/EMBO meeting Philadelphia, USA. Hartl has been a member of ASCB since 2004, Horwich since 1991. [more]
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Cellular power outage

October 26, 2017

A common feature of neurodegenerative diseases such as Alzheimer's, Parkinson's or Huntington's disease are deposits of aggregated proteins in the patient's cells that cause damage to cellular functions. Scientists at the Max Planck Institute of Biochemistry and Ludwig-Maximilians-Universität (LMU) in Munich report that, even in normal cells, aberrant aggregation-prone proteins are continually produced due to partial failure of the respiratory system. Unless they are removed by degradation, aggregates accumulate preferentially in the mitochondria, the cellular power plants, ultimately blocking energy production. In order to get rid of these toxic aggregates, cells have developed an elaborate protein quality control system, which the researchers now describe in the journal Cell.

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Ernst Schering Prize for F.-Ulrich Hartl

September 06, 2016

The Ernst Schering Foundation has honored cell biologist F.-Ulrich Hartl, director at the Max Planck Institute of Biochemistry in Martinsried near Munich, for his outstanding research on the role of chaperones in protein folding in living cells. The 50,000-euro Ernst Schering Prize is one of the most prestigious German science prizes. Professor Sies, who will give the presentation speech at the award ceremony, comments: “Franz-Ulrich Hartl’s outstanding research deserves the highest recognition. It combines fundamental new insights into the homeostasis of correctly folded proteins with new perspectives on the development and progression of neurodegenerative diseases, which may lead to innovative therapeutic approaches.” The celebratory award ceremony will take place on September 26, 2016, in Berlin. Just few weeks ago it was also announced that Hartl will receive, together with Arthur L. Horwich and Susan L. Lindquist, this years’ Albany Medical Center Prize, one of America’s most distinguished Prizes in Medicine.

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Albany Medical Center Prize for F.-Ulrich Hartl

August 03, 2016

F.-Ulrich Hartl, director at the Max Planck Institute of Biochemistry in Martinsried near Munich, will receive, together with Arthur L. Horwich and Susan L. Lindquist, this year’s Albany Medical Center Prize. The Albany Medical and Research Prize is endowed with $ 500,000 (450,000 €) and is one of America’s most distinguished Prizes in Medicine. The three awardees were honored for their fundamental and complementary discoveries related to the mechanism of protein folding. The prize will be awarded on September 28 in Albany, NY, USA.

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Max Planck Foundation pledges one million euros to scientists

April 25, 2016

Two Research Groups from the Max Planck Institute of Biochemistry in Martinsried are set to receive approximately one million euros from the Max Planck Foundation to fund an innovative research approach. F.-Ulrich Hartl, an expert in neurodegenerative diseases, and Ralf Jungmann, who has developed the super-high resolution microscopy method DNA-PAINT, plan to combine their expertise. The researchers would like to make the complex network of proteins involved in the pathological process of Alzheimer’s disease visible. DNA-PAINT can visualize the unknown molecular interactions at a high spatial resolution, thereby providing the basis for the development of new therapeutic approaches.

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How toxic protein aggregates develop

February 29, 2016

Protein aggregates are deemed to be one reason for the death of nerve cells in disorders such as Alzheimer's or Huntington's disease. As researchers at the Max Planck Institute of Biochemistry report in the current issue of Nature, they have now decoded a new cellular mechanism for the development of aggregates. Missing stop signals in the production of proteins lead erroneously to long lysine chains at the end of the protein. This in turn blocks the ribosomes, the cell's protein factory. Healthy cells detect blocked ribosomes and rapidly destroy useless proteins. If the necessary quality control machinery does not function properly, defective proteins accumulate and form toxic aggregates.

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HSF1 – in case of emergency

February 15, 2016

Just as we humans do well to call the police or fire services in the event of an emergency, cells have helpers that are activated in a crisis. Cellular stress activates heat-shock transcription factor 1 (HSF1), which then binds DNA and facilitates the production of the cellular helpers. Researchers from the Max Planck Institute of Biochemistry in Martinsried have managed to demonstrate how this process works. Using X-ray crystallography, the scientists have decoded the exact structure of HSF1 and are thus able to explain the protein’s operating mode. Their work was recently published in the journal Nature Structural & Molecular Biology.

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Why nerve cells die

January 11, 2016

For over 100 years medical researchers have observed protein deposits, also called aggregates, in the brains of patients with neurodegenerative diseases like Alzheimer’s, Parkinson’s or Huntington’s Disease as well as amyotrophic lateral sclerosis (ALS). These aggregates are suspected to contribute to the death of nerve cells. Scientists from the Max Planck Institute of Biochemistry in Martinsried, led by Mark Hipp and Ulrich Hartl, have now shown that the location of protein aggregates strongly influences the survival of cells. While aggregates within the nucleus barely influence cellular function, deposits of identical proteins within the cytoplasm interfere with important transport routes between the nucleus and the cytoplasm. In the long run this can lead to the death of the affected cells, and progression of the disease. The results of these studies have now been published in the journal Science.

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Protein aggregates save cells during aging

May 07, 2015
As an organism ages, a gradual loss of cellular protein quality control occurs. This results in the increased production of toxic protein clumps, so-called aggregates. Using a comprehensive approach, researchers in the teams of F.-Ulrich Hartl and Matthias Mann at the MPI of Biochemistry now analyzed the changes in protein composition during aging. The results published in the journal Cell show that the quantities of proteins undergo a severe shift. This also sheds new light on the origin and function of protein aggregates. The study also involves the groups of Michele Vendruscolo and Chris Dobson in Cambridge and of Richard Morimoto in Chicago. [more]
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Emergency Alert in the Cell

February 28, 2014
After a natural disaster like a big fire, countless helpers work together to get rid of debris, to build temporary shelters and to provide food for people in need. When a cell is exposed to dangerous environmental conditions such as high temperatures or toxic substances, a quite similar process is initiated: the cellular stress response, also called heat shock response. Together with colleagues from the Technical University of Dresden, scientists of the Max Planck Institute of Biochemistry in Munich-Martinsried could uncover an entire network of cellular helpers and thus identify new regulatory mechanisms of this stress response. “Our results could also be of use for investigating neurodegenerative diseases such as Alzheimer’s or Parkinson’s,” hopes Christian Loew, PhD student at the MPI of Biochemistry. The study has now been published in the Journal Cell. [more]
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Blockade in Cellular Waste Disposal - Max Planck Scientists Show How Protein Aggregates Disrupt the Molecular Balance of the Cell

June 21, 2013
Proteins can only perform their complex functions in the cell when they assume a specific three-dimensional structure for each respective task. Because misfolded proteins are often toxic, they are immediately refolded or degraded. Scientists of the Max Planck Institute (MPI) of Biochemistry in Martinsried near Munich have now shown in the yeast model that specific protein aggregates block an important degradation pathway for defective proteins – and thus disrupt the fragile molecular balance of the cell. The results of the study have now been published in the journal Cell. [more]
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EU Grant Awarded for Dementia Research - Max Planck Researchers receive 13.9 Million Euros in EU funding

December 18, 2012
Neurodegenerative diseases such as Alzheimer's, Parkinson's, Huntington's disease and amyotrophic lateral sclerosis (ALS) are characterized by toxic protein aggregates in certain regions of the brain and nerve cells. The objective of the project of F.-Ulrich Hartl, Wolfgang Baumeister, Rüdiger Klein and Matthias Mann is to elucidate just how this aggregation process is linked to cytotoxicity and cell death. For their project, the four directors of the Max Planck Institutes of Biochemistry and of Neurobiology in Martinsried near Munich, Germany, have now been awarded a Synergy Grant of the European Research Council (ERC). The four professors will use the 13.9 million euros in funding to establish closely collaborating research groups throughout the project lifetime of six years. The ERC Synergy Grant is the most highly endowed research grant of the European Union and was awarded this year for the first time [more]
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Franz-Ulrich Hartl receives Shaw Prize - Award for Research on Protein Folding

May 29, 2012
Proteins are the cell’s molecular building material and machinery, and they are involved in nearly every bioprocess. Together with Arthur L. Horwich (Yale University, USA), Franz-Ulrich Hartl, director at the Max Planck Institute of Biochemistry, will be awarded the 2012 Shaw Prize in Life Sciences and Medicine for his research on protein folding. The prize comes with a shared $1,000,000 honorarium and will be awarded by the Shaw Prize Foundation on September 17, 2012. [more]
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The Dance of the Chaperones - Max Planck Scientists Identify Key Player of Protein Folding

March 08, 2012
Proteins are the molecular building blocks and machinery of cells, and are involved in practically all biological processes. To fulfill their tasks they need to be folded into a complicated three-dimensional structure. Scientists from the Max Planck Institute of Biochemistry (MPIB) in Martinsried near Munich, Germany, have now analyzed one of the key players of the folding process: the molecular chaperone DnaK. “The understanding of these mechanisms is of great interest in the light of the many diseases in which folding goes awry, such as Alzheimer’ or Parkinson’s” says Ulrich Hartl, MPIB director. Their work has now been published in Cell Reports. [more]
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Proteins: It all depends on a correct folding plan - The protein researcher Franz-Ulrich Hartl will be awarded the Heinrich Wieland Prize 2011

October 27, 2011
What do neurodegenerative diseases such as Morbus Alzheimer, Chorea Huntington and Morbus Parkinson have in common? They all occur more and more frequently in an aging society, and wrongly folded, clumped proteins play a central role in disease development. Once that scientists have successfully decoded the molecular mechanisms underlying protein folding, new approaches for the prevention, diagnosis and therapy of these illnesses could emerge. The Heinrich Wieland Prize 2011 will be awarded to Prof. Franz-Ulrich Hartl, director at the Max Planck Institute of Biochemistry in Martinsried for his pioneering work in the field of protein folding. The award is sponsored by the Boehringer Ingelheim Foundation and comes with a prize money of 50,000 Euros. [more]
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Franz-Ulrich Hartl receives Lasker Award - Award for Research on Protein Folding

September 12, 2011
Proteins are the cell’s molecular building material and machinery, and they are involved in nearly every bioprocess. Together with Arthur L. Horwich (Yale University, USA), Franz-Ulrich Hartl, director at the Max Planck Institute of Biochemistry, will be awarded the 2011 Albert Lasker Basic Medical Research Award for his research on protein folding. The prize comes with a shared $250,000 honorarium and will be awarded by the Lasker Foundation on September 23, 2011 in New York, USA. [more]
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Collapse of the Cellular Protein Network Causes Alzheimer's? - Max Planck Scientists Uncover How Protein Aggregation Can Lead to Neurodegenerative Diseases

January 19, 2011
Protein aggregation underlies several neurodegenerative diseases such as Alzheimer’s, Huntington’s chorea or Parkinson’s. Scientists at the Max Planck Institute of Biochemistry (MPIB) in Martinsried near Munich, Germany, now discovered a fundamental mechanism which explains how toxic protein aggregation occurs and why it leads to a widespread impairment of essential cellular functions. “Not all proteins are affected by aggregation”, says Heidi Olzscha, PhD student at the MPIB. “Especially those proteins are susceptible, which possess specific structural characteristics and are involved in important biological processes.” (Cell, January 7, 2011) [more]
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protein folding

October 18, 2010
Proteins are chain-like molecules. In order to function properly, they must fold into complex three-dimensional shapes. The failure of proteins to fold properly has been linked to various diseases, including cancer, Huntington’s disease and Alzheimer’s disease. Understanding protein folding will aid the development of therapies that remove or prevent the formation of misfolded protein clumps. [more]
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Franz-Ulrich Hartl receives Heineken Prize -Award for Research on Protein Folding

April 16, 2010
Proteins are the cell’s molecular building material and machineries, and they are involved in nearly every bioprocess. For his research on protein folding Franz-Ulrich Hartl, director at the Max Planck Institute of Biochemistry, will be awarded the Dr H.P. Heineken Prize for Biochemistry and Biophysics. The prize is associated with a prize money amounting to 150,000 dollars and will be awarded by the Royal Netherlands Academy of Arts and Sciences (KNAW) on September 23, 2010 in Amsterdam. [more]
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Franz-Ulrich Hartl receives Otto Warburg Medal - Award for Research on Protein Folding

September 28, 2009
For his research on protein folding, Franz-Ulrich Hartl, Director at the Max Planck Institute of Biochemistry in Martinsried near Munich, Germany, has now been awarded with the Otto Warburg Medal. The prize was presented to him during the international meeting entitled “Signal Transduction and Disease”. [more]

Efficient working in confined spaces - New insights into the architecture of cellular protein factories

January 23, 2009
Each cell in an organism possesses its own protein factories known as ribosomes. Every second, these enzyme complexes produce new proteins with messenger molecules (mRNA) from the cell nucleus as blueprints. In order to generate as many proteins as possible at the same time, several ribosomes cluster together to form an “industrial complex” – the polysome - and read simultaneously the same messenger molecule. Scientists at the Max-Planck-Institute of Biochemistry have now, for the first time, been able to reveal the three-dimensional structure of these complexes (Cell, January 23, 2009). [more]
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Louisa Gross Horwitz Prize to Franz-Ulrich Hartl

November 20, 2008
Columbia University will award this year's Louisa Gross Horwitz Prize to Franz-Ulrich Hartl, M.D., professor and director of the Department of Cellular Biochemistry, on November 25, 2008. Hartl will be honored together with Arthur Horwich, Yale University School of Medicine, for their collaborative work in expanding fundamental understanding of cellular protein folding. [more]

Structure and Function of RbcX, an Assembly Chaperone for Hexadecameric Rubisco

June 15, 2007
Scientists from the Department of Cellular Biochemistry (F.-U. Hartl) describe the role of RbcX as an assembly chaperone of ribulose-bisphosphate carboxylase/oxygenase (Rubisco), the enzyme responsible for the fixation of atmospheric carbon dioxide. In cyanobacteria and plants, Rubisco is an ~520 kDa complex composed of eight large subunits (RbcL) and eight small subunits ((RbcS). [more]

New Technologies for Proteomics Research - EU-funding for international proteomics research project / Max Planck Institute for Biochemisty, Martinsried/Germany, coordinates the project

March 11, 2004
"INTERACTION PROTEOME" is the largest EU-funded project in the field of proteomics to date. The "Integrated Project" brings together the scientific excellence of eleven leading European research institutions and companies, including the largest European manufacturers of mass spectrometers and electron microscopes. The project will be funded with a total of 12 Million Euros for five years within the Research Framework Programme 6 of the European Commission to develop novel technologies for proteomics research. The project consortium celebrated the official opening of "INTERACTION PROTEOME" together with representatives of the European Commission during the "kick-off meeting" in Rome end of January 2004. [more]
 
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