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189 results on '"Liberek, Krzysztof"'

1. J-domain proteins: From molecular mechanisms to diseases.

Author

Marszalek, Jaroslaw, De Los Rios, Paolo, Cyr, Douglas, Mayer, Matthias, Adupa, Vasista, Andréasson, Claes, Blatch, Gregory, Braun, Janice, Brodsky, Jeffrey, Bukau, Bernd, Chapple, J, Conz, Charlotte, Dementin, Sébastien, Genevaux, Pierre, Genest, Olivier, Goloubinoff, Pierre, Gestwicki, Jason, Hammond, Colin, Hines, Justin, Ishikawa, Koji, Joachimiak, Lukasz, Kirstein, Janine, Liberek, Krzysztof, Mokranjac, Dejana, Nillegoda, Nadinath, Ramos, Carlos, Rebeaud, Mathieu, Ron, David, Rospert, Sabine, Sahi, Chandan, Shalgi, Reut, Tomiczek, Bartlomiej, Ushioda, Ryo, Ustyantseva, Elizaveta, Ye, Yihong, Zylicz, Maciej, and Kampinga, Harm

Subjects
Evolution, Hsp70 cycle, JDP, HSP70 Heat-Shock Proteins, Molecular Chaperones, Poland, HSP40 Heat-Shock Proteins
Abstract

J-domain proteins (JDPs) are the largest family of chaperones in most organisms, but much of how they function within the network of other chaperones and protein quality control machineries is still an enigma. Here, we report on the latest findings related to JDP functions presented at a dedicated JDP workshop in Gdansk, Poland. The report does not include all (details) of what was shared and discussed at the meeting, because some of these original data have not yet been accepted for publication elsewhere or represented still preliminary observations at the time.

Published
2024

2. The beauty and complexity of the small heat shock proteins: a report on the proceedings of the fourth workshop on small heat shock proteins.

Author

Ecroyd, Heath, Bartelt-Kirbach, Britta, Ben-Zvi, Anat, Bonavita, Raffaella, Bushman, Yevheniia, Casarotto, Elena, Cecconi, Ciro, Lau, Wilson, Hibshman, Jonathan, Joosten, Joep, Klevit, Rachel, Liberek, Krzysztof, McMenimen, Kathryn, Miwa, Tsukumi, Mogk, Axel, Montepietra, Daniele, Peters, Carsten, Rocchetti, Maria, Saman, Dominik, Sisto, Angela, Secco, Valentina, Strauch, Annika, Taguchi, Hideki, Tanguay, Morgan, Tedesco, Barbara, Toth, Melinda, Wang, Zihao, Benesch, Justin, Carra, Serena, and Kimonis, Virginia

Subjects
Cellular stress, Molecular chaperones, Protein aggregation, Protein folding, Protein homeostasis, Small heat shock proteins, Heat-Shock Proteins, Small, Proteins
Abstract

The Fourth Cell Stress Society International workshop on small heat shock proteins (sHSPs), a follow-up to successful workshops held in 2014, 2016 and 2018, took place as a virtual meeting on the 17-18 November 2022. The meeting was designed to provide an opportunity for those working on sHSPs to reconnect and discuss their latest work. The diversity of research in the sHSP field is reflected in the breadth of topics covered in the talks presented at this meeting. Here we summarise the presentations at this meeting and provide some perspectives on exciting future topics to be addressed in the field.

Published
2023

5. Function, evolution, and structure of J-domain proteins

Author

Kampinga, Harm H, Andreasson, Claes, Barducci, Alessandro, Cheetham, Michael E, Cyr, Douglas, Emanuelsson, Cecilia, Genevaux, Pierre, Gestwicki, Jason E, Goloubinoff, Pierre, Huerta-Cepas, Jaime, Kirstein, Janine, Liberek, Krzysztof, Mayer, Matthias P, Nagata, Kazuhiro, Nillegoda, Nadinath B, Pulido, Pablo, Ramos, Carlos, De los Rios, Paolo, Rospert, Sabine, Rosenzweig, Rina, Sahi, Chandan, Taipale, Mikko, Tomiczek, Bratłomiej, Ushioda, Ryo, Young, Jason C, Zimmermann, Richard, Zylicz, Alicja, Zylicz, Maciej, Craig, Elizabeth A, and Marszalek, Jaroslaw

Subjects
Biochemistry and Cell Biology, Biological Sciences, Underpinning research, 1.1 Normal biological development and functioning, Generic health relevance, Animals, Disease, Evolution, Molecular, HSP70 Heat-Shock Proteins, Humans, Protein Aggregates, Protein Domains, Protein Refolding, Heat shock protein 70, J-domain proteins, 8-stranded -sandwich domain, 8-stranded β-sandwich domain, Biochemistry & Molecular Biology, Biochemistry and cell biology
Abstract

Hsp70 chaperone systems are very versatile machines present in nearly all living organisms and in nearly all intracellular compartments. They function in many fundamental processes through their facilitation of protein (re)folding, trafficking, remodeling, disaggregation, and degradation. Hsp70 machines are regulated by co-chaperones. J-domain containing proteins (JDPs) are the largest family of Hsp70 co-chaperones and play a determining role functionally specifying and directing Hsp70 functions. Many features of JDPs are not understood; however, a number of JDP experts gathered at a recent CSSI-sponsored workshop in Gdansk (Poland) to discuss various aspects of J-domain protein function, evolution, and structure. In this report, we present the main findings and the consensus reached to help direct future developments in the field of Hsp70 research.

Published
2019

9. J-domain proteins:From molecular mechanisms to diseases

Author

Marszalek, Jaroslaw, De Los Rios, Paolo, Cyr, Douglas, Mayer, Matthias P., Adupa, Vasista, Andréasson, Claes, Blatch, Gregory L., Braun, Janice E.A., Brodsky, Jeffrey L., Bukau, Bernd, Chapple, J. Paul, Conz, Charlotte, Dementin, Sébastien, Genevaux, Pierre, Genest, Olivier, Goloubinoff, Pierre, Gestwicki, Jason, Hammond, Colin M., Hines, Justin K., Ishikawa, Koji, Joachimiak, Lukasz A., Kirstein, Janine, Liberek, Krzysztof, Mokranjac, Dejana, Nillegoda, Nadinath, Ramos, Carlos H.I., Rebeaud, Mathieu, Ron, David, Rospert, Sabine, Sahi, Chandan, Shalgi, Reut, Tomiczek, Bartlomiej, Ushioda, Ryo, Ustyantseva, Elizaveta, Ye, Yihong, Zylicz, Maciej, Kampinga, Harm H., Marszalek, Jaroslaw, De Los Rios, Paolo, Cyr, Douglas, Mayer, Matthias P., Adupa, Vasista, Andréasson, Claes, Blatch, Gregory L., Braun, Janice E.A., Brodsky, Jeffrey L., Bukau, Bernd, Chapple, J. Paul, Conz, Charlotte, Dementin, Sébastien, Genevaux, Pierre, Genest, Olivier, Goloubinoff, Pierre, Gestwicki, Jason, Hammond, Colin M., Hines, Justin K., Ishikawa, Koji, Joachimiak, Lukasz A., Kirstein, Janine, Liberek, Krzysztof, Mokranjac, Dejana, Nillegoda, Nadinath, Ramos, Carlos H.I., Rebeaud, Mathieu, Ron, David, Rospert, Sabine, Sahi, Chandan, Shalgi, Reut, Tomiczek, Bartlomiej, Ushioda, Ryo, Ustyantseva, Elizaveta, Ye, Yihong, Zylicz, Maciej, and Kampinga, Harm H.

Abstract

J-domain proteins (JDPs) are the largest family of chaperones in most organisms, but much of how they function within the network of other chaperones and protein quality control machineries is still an enigma. Here, we report on the latest findings related to JDP functions presented at a dedicated JDP workshop in Gdansk, Poland. The report does not include all (details) of what was shared and discussed at the meeting, because some of these original data have not yet been accepted for publication elsewhere or represented still preliminary observations at the time.

Published
2024

12. Small heat shock proteins: multifaceted proteins with important implications for life

Author

Carra, Serena, Alberti, Simon, Benesch, Justin L. P., Bolens, Wilbert, Buchner, Johannes, Carver, John A., Cecconi, Ciro, Ecroyd, Heath, Gusev, Nikolai, Hightower, Lawrence E., Klevit, Rachel E., Lee, Hyun O., Liberek, Krzysztof, Lockwood, Brent, Poletti, Angelo, Timmerman, Vincent, Toth, Melinda E., Vierling, Elizabeth, Wu, Tangchun, and Tanguay, Robert M.

Published
2019
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13. The growing world of small heat shock proteins: from structure to functions

Author

Carra, Serena, Alberti, Simon, Arrigo, Patrick A., Benesch, Justin L., Benjamin, Ivor J., Boelens, Wilbert, Bartelt-Kirbach, Britta, Brundel, Bianca J. J. M., Buchner, Johannes, Bukau, Bernd, Carver, John A., Ecroyd, Heath, Emanuelsson, Cecilia, Finet, Stephanie, Golenhofen, Nikola, Goloubinoff, Pierre, Gusev, Nikolai, Haslbeck, Martin, Hightower, Lawrence E., Kampinga, Harm H., Klevit, Rachel E., Liberek, Krzysztof, Mchaourab, Hassane S., McMenimen, Kathryn A., Poletti, Angelo, Quinlan, Roy, Strelkov, Sergei V., Toth, Melinda E., Vierling, Elizabeth, and Tanguay, Robert M.

Published
2017

18. Disruption of Ionic Interactions between the Nucleotide Binding Domain 1 (NBD1) and Middle (M) Domain in Hsp100 Disaggregase Unleashes Toxic Hyperactivity and Partial Independence from Hsp70

Author

Lipińska, Natalia, Ziętkiewicz, Szymon, Sobczak, Alicja, Jurczyk, Agnieszka, Potocki, Wojciech, Morawiec, Ewa, Wawrzycka, Aleksandra, Gumowski, Krzysztof, Ślusarz, Magdalena, Rodziewicz-Motowidło, Sylwia, Chruściel, Elżbieta, and Liberek, Krzysztof

Published
2013
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32. Formation of the preprimosome protects lambda O from RNA transcription-dependent proteolysis by ClpP/Clpx

Author

Zylicz, Maciej, Liberek, Krzysztof, Wawrzynow, Alicja, and Georgopoulos, Costa

Subjects
Bacteriophages -- Research, DNA -- Research, Genetic transcription -- Research, Proteolysis -- Research, Proteases -- Research, RNA -- Research, Science and technology
Abstract

Using the bacteriophage [Lambda] DNA replication system, composed entirely of purified proteins, we have tested the accessibility of the short-lived [Lambda] O protein to the ClpP/ClpX protease during the various stages of [Lambda] DNA replication. We find that binding of [Lambda] O protein to its ori[Lambda] DNA sequence, leading to the so-called 'O-some' formation, largely inhibits its degradation. On the contrary, under conditions permissive for transcription, the [Lambda] O protein bound to the ori[Lambda] sequence becomes largely accessible to ClpP/ClpX-mediated proteolysis. However, when the [Lambda] O protein is part of the larger ori[Lambda]:O[center dot]P[center dot]DnaB preprimosomal complex, transcription does not significantly increase ClpP/ClpX-dependent [Lambda] O degradation. These results show that transcription can stimulate proteolysis of a protein that is required for the initiation of DNA replication.

Published
1998

34. The DnaJ chaperone catalytically activates the DnaK chaperone to preferentially bind the sigma(super 32) heat shock transcriptional regulator

Author

Liberek, Krzysztof, Wall, Daniel, and Georgopoulos, Costa

Subjects
Genetic transcription -- Regulation, Proteins -- Analysis, DNA -- Research, Bacteriophages -- Genetic aspects, Science and technology
Abstract

DnaJ protein can catalytically actuate DnaK's ATPase activity and can also activate DnaK to bind to sigma(super 32) in an ATP-dependent reaction, forming a stable sigma(super 32)-DnaK complex. Results obtained from two DnaJ mutants indicate that the N-terminal portion of DnaJ is essential for this activation reaction. The activated form of DnaK binds preferentially to sigma(super 32) versus the lambdaP protein substrate. DnaK and DnaJ proteins compete with RNA polymerase for binding to the sigma(super 32) transcription factor to form a stable DnaJ-sigma(super 32)-DnaK protein complex.

Published
1995

35. The DNaK chaperone modulates the heat shock response of Escherichia coli by binding to the sigma(super 32) transcription factor

Author

Liberek, Krzysztof, Galitski, Timothy P., Zylicz, Maciej, and Georgopoulos, Costa

Subjects
Genetic transcription -- Regulation, Escherichia coli -- Physiological aspects, Heat shock proteins -- Genetic aspects, Science and technology
Abstract

The sigma(super 32) polypeptide is involved in the positive regulation of the heat shock genes of Escherichia coli. The possible association of this sigma factor to the DnaK chaperone protein was studied. Sigma(super 32) was purified to homogeneity and subjected to binding assays. The results showed that wild-type DnaK is capable of binding to sigma(super 32). This association suggests that DnaK modulates the expression of heat shock genes by sequestering sigma(super 32).

Published
1992

40. Function, evolution, and structure of J-domain proteins

Author

Kampinga, Harm H., Andreasson, Claes, Barducci, Alessandro, Cheetham, Michael E., Cyr, Douglas, Emanuelsson, Cecilia, Genevaux, Pierre, Gestwicki, Jason E., Goloubinoff, Pierre, Huerta-Cepas, Jaime, Kirstein, Janine, Liberek, Krzysztof, Mayer, Matthias P., Nagata, Kazuhiro, Nillegoda, Nadinath B., Pulido, Pablo, Ramos, Carlos, De los Rios, Paolo, Rospert, Sabine, Rosenzweig, Rina, Sahi, Chandan, Taipale, Mikko, Tomiczek, Bratlomiej, Ushioda, Ryo, Young, Jason C., Zimmermann, Richard, Zylicz, Alicja, Zylicz, Maciej, Craig, Elizabeth A., Marszalek, Jaroslaw, Kampinga, Harm H., Andreasson, Claes, Barducci, Alessandro, Cheetham, Michael E., Cyr, Douglas, Emanuelsson, Cecilia, Genevaux, Pierre, Gestwicki, Jason E., Goloubinoff, Pierre, Huerta-Cepas, Jaime, Kirstein, Janine, Liberek, Krzysztof, Mayer, Matthias P., Nagata, Kazuhiro, Nillegoda, Nadinath B., Pulido, Pablo, Ramos, Carlos, De los Rios, Paolo, Rospert, Sabine, Rosenzweig, Rina, Sahi, Chandan, Taipale, Mikko, Tomiczek, Bratlomiej, Ushioda, Ryo, Young, Jason C., Zimmermann, Richard, Zylicz, Alicja, Zylicz, Maciej, Craig, Elizabeth A., and Marszalek, Jaroslaw

Abstract

Hsp70 chaperone systems are very versatile machines present in nearly all living organisms and in nearly all intracellular compartments. They function in many fundamental processes through their facilitation of protein (re)folding, trafficking, remodeling, disaggregation, and degradation. Hsp70 machines are regulated by co-chaperones. J-domain containing proteins (JDPs) are the largest family of Hsp70 co-chaperones and play a determining role functionally specifying and directing Hsp70 functions. Many features of JDPs are not understood; however, a number of JDP experts gathered at a recent CSSI-sponsored workshop in Gdansk (Poland) to discuss various aspects of J-domain protein function, evolution, and structure. In this report, we present the main findings and the consensus reached to help direct future developments in the field of Hsp70 research.

Published
2019
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45. Function, evolution, and structure of J-domain proteins

Author

Kampinga, Harm H., primary, Andreasson, Claes, additional, Barducci, Alessandro, additional, Cheetham, Michael E., additional, Cyr, Douglas, additional, Emanuelsson, Cecilia, additional, Genevaux, Pierre, additional, Gestwicki, Jason E., additional, Goloubinoff, Pierre, additional, Huerta-Cepas, Jaime, additional, Kirstein, Janine, additional, Liberek, Krzysztof, additional, Mayer, Matthias P., additional, Nagata, Kazuhiro, additional, Nillegoda, Nadinath B., additional, Pulido, Pablo, additional, Ramos, Carlos, additional, De los Rios, Paolo, additional, Rospert, Sabine, additional, Rosenzweig, Rina, additional, Sahi, Chandan, additional, Taipale, Mikko, additional, Tomiczek, Bratłomiej, additional, Ushioda, Ryo, additional, Young, Jason C., additional, Zimmermann, Richard, additional, Zylicz, Alicja, additional, Zylicz, Maciej, additional, Craig, Elizabeth A., additional, and Marszalek, Jaroslaw, additional

Published
2018
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