scholarly journals Auto-regulatory J-domain interactions control Hsp70 recruitment to the DnaJB8 chaperone

2020 ◽  
Author(s):  
Bryan D. Ryder ◽  
Irina Matlahov ◽  
Sofia Bali ◽  
Jaime Vaquer-Alicea ◽  
Patrick C.A. van der Wel ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Protein Aggregation ◽  
Regulatory Element ◽  
Structure And Function ◽  
High Substrate ◽  
Evolutionarily Conserved ◽  
Hsp70 Chaperone ◽  
Domain Interactions ◽  
J Domain ◽  
And Function

AbstractThe Hsp40/Hsp70 chaperone families combine versatile folding capacity with high substrate specificity, which is mainly facilitated by Hsp40s. The structure and function of many Hsp40s remain poorly understood, particularly oligomeric Hsp40s that suppress protein aggregation. Here, we used a combination of biochemical and structural approaches to shed new light on the domain interactions of the Hsp40 DnaJB8, and how they regulate recruitment of partner Hsp70s. We identify an interaction between the J-Domain (JD) and C-terminal domain (CTD) of DnaJB8 that sequesters the JD surface, preventing Hsp70 interaction. We propose a new model for DnaJB8-Hsp70 regulation, whereby the JD-CTD interaction of DnaJB8 acts as a reversible autoinhibitory switch that can control the binding of Hsp70. These findings suggest that the evolutionarily conserved CTD of DnaJB8 is a regulatory element of chaperone activity in the proteostasis network.

scholarly journals Regulatory inter-domain interactions influence Hsp70 recruitment to the DnaJB8 chaperone

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Bryan D. Ryder ◽  
Irina Matlahov ◽  
Sofia Bali ◽  
Jaime Vaquer-Alicea ◽  
Patrick C. A. van der Wel ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Protein Aggregation ◽  
Regulatory Element ◽  
Structure And Function ◽  
Evolutionarily Conserved ◽  
Hsp70 Chaperone ◽  
Domain Interactions ◽  
J Domain ◽  
And Function ◽  
Shed Light

AbstractThe Hsp40/Hsp70 chaperone families combine versatile folding capacity with high substrate specificity, which is mainly facilitated by Hsp40s. The structure and function of many Hsp40s remain poorly understood, particularly oligomeric Hsp40s that suppress protein aggregation. Here, we used a combination of biochemical and structural approaches to shed light on the domain interactions of the Hsp40 DnaJB8, and how they may influence recruitment of partner Hsp70s. We identify an interaction between the J-Domain (JD) and C-terminal domain (CTD) of DnaJB8 that sequesters the JD surface, preventing Hsp70 interaction. We propose a model for DnaJB8-Hsp70 recruitment, whereby the JD-CTD interaction of DnaJB8 acts as a reversible switch that can control the binding of Hsp70. These findings suggest that the evolutionarily conserved CTD of DnaJB8 is a regulatory element of chaperone activity in the proteostasis network.

scholarly journals Structure and Function of the  -globin Upstream Regulatory Element

1996 ◽  
Vol 24 (24) ◽  
pp. 4978-4986 ◽  
Author(s):  
D. E. Sabath ◽  
K. M. Koehler ◽  
W.-Q. Yang
Keyword(s):  
Regulatory Element ◽  
Structure And Function ◽  
Upstream Regulatory Element ◽  
And Function

scholarly journals Recent progress in research on molecular mechanisms of autophagy in the heart

2015 ◽  
Vol 308 (4) ◽  
pp. H259-H268 ◽  
Author(s):  
Yasuhiro Maejima ◽  
Yun Chen ◽  
Mitsuaki Isobe ◽  
Åsa B. Gustafsson ◽  
Richard N. Kitsis ◽  
...  
Keyword(s):  
Heart Disease ◽  
Molecular Mechanisms ◽  
Therapeutic Potential ◽  
Degradation Process ◽  
Structure And Function ◽  
Cellular Functions ◽  
Evolutionarily Conserved ◽  
And Function ◽  
Cellular Dysfunction

Dysregulation of autophagy, an evolutionarily conserved process for degradation of long-lived proteins and organelles, has been implicated in the pathogenesis of human disease. Recent research has uncovered pathways that control autophagy in the heart and molecular mechanisms by which alterations in this process affect cardiac structure and function. Although initially thought to be a nonselective degradation process, autophagy, as it has become increasingly clear, can exhibit specificity in the degradation of molecules and organelles, such as mitochondria. Furthermore, it has been shown that autophagy is involved in a wide variety of previously unrecognized cellular functions, such as cell death and metabolism. A growing body of evidence suggests that deviation from appropriate levels of autophagy causes cellular dysfunction and death, which in turn leads to heart disease. Here, we review recent advances in understanding the role of autophagy in heart disease, highlight unsolved issues, and discuss the therapeutic potential of modulating autophagy in heart disease.

scholarly journals Structure and function of yeast alcohol dehydrogenase

2000 ◽  
Vol 65 (4) ◽  
pp. 207-227 ◽  
Author(s):  
Svetlana Trivic ◽  
Vladimir Leskovac
Keyword(s):  
Alcohol Dehydrogenase ◽  
Substrate Specificity ◽  
Primary Structure ◽  
Active Site ◽  
Hydride Transfer ◽  
Kinetic Mechanism ◽  
Structure And Function ◽  
Chemical Mechanism ◽  
And Function ◽  
Font Color

1. Introduction 2. Isoenzymes of YADH 3. Substrate specificity 4. Kinetic mechanism 5. Primary structure 6. The active site 7. Mutations in the yeast enzyme 8. Chemical mechanism 9. Binding of coenzymes 10. Hydride transfer <br><br><font color="red"><b> This article has been corrected. Link to the correction <u><a href="http://dx.doi.org/10.2298/JSC0008609E">10.2298/JSC0008609E</a><u></b></font>

scholarly journals Integrated Structural Modeling of Full-Length LRH-1 Reveals Inter-domain Interactions Contribute to Receptor Structure and Function

Structure ◽  
2020 ◽  
Vol 28 (7) ◽  
pp. 830-846.e9
Author(s):  
Corey D. Seacrist ◽  
Georg Kuenze ◽  
Reece M. Hoffmann ◽  
Brandon E. Moeller ◽  
John E. Burke ◽  
...  
Keyword(s):  
Structural Modeling ◽  
Structure And Function ◽  
Full Length ◽  
Receptor Structure ◽  
Domain Interactions ◽  
And Function

Structure and function of the MRNA iron regulatory element(IRE)

1993 ◽  
Vol 51 (1-2) ◽  
pp. 586
Author(s):  
A.R. McKenzie ◽  
H. Sierzputowska-Grascz ◽  
D.R. Dix ◽  
L-P. Nain ◽  
E.C. Theil
Keyword(s):  
Regulatory Element ◽  
Structure And Function ◽  
And Function ◽  
Iron Regulatory Element

[NiFe]-Hydrogenase maturation endopeptidase: structure and function

2005 ◽  
Vol 33 (1) ◽  
pp. 108-111 ◽  
Author(s):  
E. Theodoratou ◽  
R. Huber ◽  
A. Böck
Keyword(s):  
Reaction Mechanism ◽  
Substrate Specificity ◽  
Large Subunit ◽  
Cysteine Residue ◽  
Structure And Function ◽  
Metal Centre ◽  
Conformational Switch ◽  
Hydrogenase Maturation ◽  
And Function

Hydrogenase maturation endopeptidases catalyse the terminal step in the maturation of the large subunit of [NiFe]-hydrogenases. They remove a C-terminal extension from the precursor of the subunit, triggering a conformational switch that results in the bridging of the Fe and Ni atoms of the metal centre via the thiolate of a cysteine residue and in closure of the centre. This review summarizes what is known about the structure of the protein, its substrate specificity and its possible reaction mechanism.

scholarly journals Meiotic condensin is required for proper chromosome compaction, SC assembly, and resolution of recombination-dependent chromosome linkages

2003 ◽  
Vol 163 (5) ◽  
pp. 937-947 ◽  
Author(s):  
Hong-Guo Yu ◽  
Douglas E. Koshland
Keyword(s):  
Mitotic Chromosome ◽  
Chromosome Structure ◽  
Chromosomal Localization ◽  
Meiotic Chromosome ◽  
Chromosome Condensation ◽  
Structure And Function ◽  
Double Strand Breaks ◽  
Strand Breaks ◽  
Evolutionarily Conserved ◽  
And Function

Condensin is an evolutionarily conserved protein complex that helps mediate chromosome condensation and segregation in mitotic cells. Here, we show that condensin has two activities that contribute to meiotic chromosome condensation in Saccharomyces cerevisiae. One activity, common to mitosis, helps mediate axial length compaction. A second activity promotes chromosome individualization with the help of Red1 and Hop1, two meiotic specific components of axial elements. Like Red1 and Hop1, condensin is also required for efficient homologue pairing and proper processing of double strand breaks. Consistent with these functional links condensin is necessary for proper chromosomal localization of Red1 and Hop1 and the subsequent assembly of the synaptonemal complex. Finally, condensin has a Red1/Hop1-independent role in the resolution of recombination-dependent linkages between homologues in meiosis I. The existence of distinct meiotic activities of condensin (axial compaction, individualization, and resolution of recombination-dependent links) provides an important framework to understand condensin's role in both meiotic and mitotic chromosome structure and function.

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