4.4 Article

The influence of ATP-dependent proteases on a variety of nucleoid-associated processes

期刊

JOURNAL OF STRUCTURAL BIOLOGY
卷 179, 期 2, 页码 181-192

出版社

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2012.05.018

关键词

ATP-dependent proteases; Lon; ClpAP; ClpXP; HslUV; FtsH; DNA-binding proteins; Nucleoid; Bacterial DNA; Mitochondrial DNA

资金

  1. Slovak Research and Development Agency [APVV-0123-10]
  2. Slovak Grant Agency [VEGA 2/0122/11]
  3. Academy of Sciences of the Czech Republic [RVO: 61388971]

向作者/读者索取更多资源

ATP-dependent proteases are crucial components of all living cells and are involved in a variety of responses to physiological and environmental changes. Nucleoids are dynamic nucleoprotein complexes present in bacteria and eukaryotic organelles (mitochondria and plastids) and are the place where the majority of cellular responses to stress begin. These structures are actively remodeled in reaction to changing environmental and physiological conditions. The levels of nucleoid protein components (e.g. DNA-stabilizing proteins, transcription factors, replication proteins) therefore have to be continually regulated. ATP-dependent proteases have all the characteristics needed to fulfill this requirement. Some of them bind nucleic acids, but above all, they control and maintain the level of many DNA-binding proteins. In this review we will discuss the roles of the Lon, ClpAP, ClpXP, HslUV and FtsH proteases in the maintenance, stability, transcription and repair of DNA in eubacterial and mitochondrial nucleoids. (C) 2012 Elsevier Inc. All rights reserved.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.4
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

Article Biochemistry & Molecular Biology

Disease-associated mutations alter the dynamic motion of the N-terminal domain of the human cardiac ryanodine receptor

Jacob A. Bauer, L'ubomir Borko, Jelena Pavlovic, Eva Kutejova, Vladena Bauerova-Hlinkova

JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS (2020)

Article Biochemistry & Molecular Biology

Yeast phosphatidylinositol transfer protein Pdr17 does not require high affinity phosphatidylinositol binding for its cellular function

Zuzana Pevalova, Vladimir Pevala, Nicholas J. Blunsom, Dana Tahotna, Veronika Kotrasova, Roman Holic, Lucia Pokorna, Jacob A. Bauer, Eva Kutejova, Shamshad Cockcroft, Peter Griac

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS (2019)

Review Biochemistry & Molecular Biology

Mitochondrial HMG-Box Containing Proteins: From Biochemical Properties to the Roles in Human Diseases

Veronika Vozarikova, Nina Kunova, Jacob A. Bauer, Jan Frankovsky, Veronika Kotrasova, Katarina Prochazkova, Vladimira Dzugasova, Eva Kutejova, Vladimir Pevala, Jozef Nosek, Lubomir Tomaska

BIOMOLECULES (2020)

Review Biology

Mitochondrial Kinases and the Role of Mitochondrial Protein Phosphorylation in Health and Disease

Veronika Kotrasova, Barbora Keresztesova, Gabriela Ondrovicova, Jacob A. Bauer, Henrieta Havalova, Vladimir Pevala, Eva Kutejova, Nina Kunova

Summary: Mitochondria play a major role in providing energy to cells and responding to stress factors and metabolic changes. Post-translational modification, such as phosphorylation, is a fast and efficient way for cells to adapt to changing conditions, but it also alters protein structure and function. Kinases, responsible for phosphorylation, have a significant impact on mitochondrial biogenesis and function under different cellular conditions.

LIFE-BASEL (2021)

Review Biochemistry & Molecular Biology

Mitochondrial HSP70 Chaperone System-The Influence of Post-Translational Modifications and Involvement in Human Diseases

Henrieta Havalova, Gabriela Ondrovicova, Barbora Keresztesova, Jacob A. Bauer, Vladimir Pevala, Eva Kutejova, Nina Kunova

Summary: Heat shock proteins (HSPs) are found in all domains of life, particularly in mitochondria where they play crucial roles in maintaining organelle function and health. The human mitochondrial HSP70 chaperone system consists of mtHSP70 or mortalin and three co-chaperones, which work together to stabilize and import nuclear gene products and regulate protein folding functions. Dysregulation of these molecular chaperones is often linked to neurological disorders, genetic diseases, and cancer.

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES (2021)

Review Biochemistry & Molecular Biology

Mitochondrial Processing Peptidases-Structure, Function and the Role in Human Diseases

Nina Kunova, Henrieta Havalova, Gabriela Ondrovicova, Barbora Stojkovicova, Jacob A. Bauer, Vladena Bauerova-Hlinkova, Vladimir Pevala, Eva Kutejova

Summary: Mitochondrial proteins are transported into mitochondria using a sophisticated system, and their proper folding and assembly rely on the cleavage of targeting presequences. Mitochondrial processing peptidases play a crucial role in mitochondrial homeostasis and their malfunctions are linked to severe human diseases.

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES (2022)

Article Biochemistry & Molecular Biology

The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids

Jan Frankovsky, Barbora Keresztesova, Jana Bellova, Nina Kunova, Nikola Canigova, Katerina Hanakova, Jacob A. Bauer, Gabriela Ondrovicova, Veronika Lukacova, Barbara Sivakova, Zbynek Zdrahal, Vladimir Pevala, Katarina Prochazkova, Jozef Nosek, Peter Barath, Eva Kutejova, Lubomir Tomaska

Summary: Acylation modifications, such as lysine succinylation, are important in regulating protein activity, with some occurring non-enzymatically due to an increase in acyl group donors. In eukaryotes, mitochondrial proteins are predominantly affected by lysine succinylation, as succinate donors are primarily generated in the tricarboxylic acid cycle. This modification can have a profound effect on protein function, as seen in the succinylation of Abf2p affecting its DNA-binding activity and sensitivity to protease digestion.

JOURNAL OF BIOLOGICAL CHEMISTRY (2021)

Article Biochemistry & Molecular Biology

Yeast Sec14-like lipid transfer proteins Pdr16 and Pdr17 bind and transfer the ergosterol precursor lanosterol in addition to phosphatidylinositol

Dominik Stastny, Livia Petriskova, Dana Tahotna, Jacob Bauer, Lucia Pokorna, Roman Holic, Martin Valachovic, Vladimir Pevala, Shamshad Cockcroft, Peter Griac

Summary: Yeast Sec14-like phosphatidylinositol transfer proteins (PITPs) have a hydrophobic cavity capable of binding and transferring lanosterol. This is the first identification of lanosterol transfer proteins. A double mutant lacking Pdr16p and Pdr17p showed increased cellular lanosterol levels, indicating the importance of PI-lanosterol transfer proteins in sterol biosynthesis.

FEBS LETTERS (2023)

Article Immunology

Cost-Effective Protein Production in CHO Cells Following Polyethylenimine-Mediated Gene Delivery Showcased by the Production and Crystallization of Antibody Fabs

Klaudia Meskova, Katarina Martonova, Patricia Hrasnova, Kristina Sinska, Michaela Skrabanova, Lubica Fialova, Stefana Njemoga, Ondrej Cehlar, Olga Parmar, Petr Kolenko, Vladimir Pevala, Rostislav Skrabana

Summary: Laboratory production of recombinant mammalian proteins, particularly antibodies, can be achieved using transient gene expression in suspension-adapted Chinese Hamster Ovary (CHO) cell lines. This method allows for secretion of antibodies into the media and can be glycosylated. However, protein production in CHO cells can be costly and variable. Optimization can be done in aspects such as gene delivery, cultivation process, and expression plasmid design. In this study, a TGE platform for medium-scale production of antibodies and other proteins in CHO cells was proposed, using a new expression vector and recyclable labware to reduce production cost. The platform's potential was demonstrated through the production and crystallization of antibody Fabs and their complexes.

ANTIBODIES (2023)

Meeting Abstract Chemistry, Multidisciplinary

HOW DISEASE-ASSOCIATED MUTATIONS MAY ALTER THE DYNAMIC MOTION OF THE N-TERMINAL DOMAIN OF THE HUMAN CARDIAC RYANODINE RECEPTOR

Jacob Bauer, Jelena Pavlovic, Eva Kutejova, Vladena Bauerova

ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES (2019)

暂无数据