Analysis of the levels of conservation of the J domain among the various types of DnaJ-like proteins

Hennessy, Fritha; Cheetham, Michael E.; Dirr, Heini W.; Blatch, Gregory L.

doi:10.1379/1466-1268(2000)005<0347:aotloc>2.0.co;2

Cited by 79 publications

(51 citation statements)

References 21 publications

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“…DnaJ proteins deliver polypeptide substrates to Hsp70 chaperones for processing and regulate chaperone activity via the interaction of their J domains with their Hsp70 partners (Bukau and Horwich, 1998;Walter and Buchner, 2002). The J domain in nearly all known DnaJ and DnaJ-like proteins contains a central His-Pro-Asp (HPD) motif, which is believed to be crucial for the interaction between the J domain and Hsp70 (Hennessy et al, 2000). However, this motif is not fully preserved in the J domains of ARC6 and its orthologs, because only the central Pro is conserved uniformly (Figure 3).…”

Section: Arc6 and Its Orthologs Encode J-domain Proteins Unique To Plmentioning

confidence: 99%

“…However, this motif is not fully preserved in the J domains of ARC6 and its orthologs, because only the central Pro is conserved uniformly (Figure 3). Conversely, other residues hypothesized to be essential for J-domain structure (Hennessy et al, 2000) are conserved (Figure 3), and a database search based on 3D-PSSM protein structure predictions (http://www. sbg.bio.ic.ac.uk/servers/3dpssm/) (Kelley et al, 2000) showed a very good fit between the ARC6-like J domains and the experimentally determined crystal structures of the J domains from human HSP40 and E. coli DnaJ.…”

Section: Arc6 and Its Orthologs Encode J-domain Proteins Unique To Plmentioning

confidence: 99%

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ARC6 Is a J-Domain Plastid Division Protein and an Evolutionary Descendant of the Cyanobacterial Cell Division Protein Ftn2[W]

et al. 2003

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Replication of chloroplasts is essential for achieving and maintaining optimal plastid numbers in plant cells. The plastid division machinery contains components of both endosymbiotic and host cell origin, but little is known about the regulation and molecular mechanisms that govern the division process. The Arabidopsis mutant arc6 is defective in plastid division, and its leaf mesophyll cells contain only one or two grossly enlarged chloroplasts. We show here that arc6 chloroplasts also exhibit abnormal localization of the key plastid division proteins FtsZ1 and FtsZ2. Whereas in wild-type plants, the FtsZ proteins assemble into a ring at the plastid division site, chloroplasts in the arc6 mutant contain numerous short, disorganized FtsZ filament fragments. We identified the mutation in arc6 and show that the ARC6 gene encodes a chloroplast-targeted DnaJ-like protein localized to the plastid envelope membrane. An ARC6-green fluorescent protein fusion protein was localized to a ring at the center of the chloroplasts and rescued the chloroplast division defect in the arc6 mutant. The ARC6 gene product is related closely to Ftn2, a prokaryotic cell division protein unique to cyanobacteria. Based on the FtsZ filament morphology observed in the arc6 mutant and in plants that overexpress ARC6 , we hypothesize that ARC6 functions in the assembly and/or stabilization of the plastid-dividing FtsZ ring. We also analyzed FtsZ localization patterns in transgenic plants in which plastid division was blocked by altered expression of the division site-determining factor AtMinD. Our results indicate that MinD and ARC6 act in opposite directions: ARC6 promotes and MinD inhibits FtsZ filament formation in the chloroplast.

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Section: Arc6 and Its Orthologs Encode J-domain Proteins Unique To Plmentioning

confidence: 99%

Section: Arc6 and Its Orthologs Encode J-domain Proteins Unique To Plmentioning

confidence: 99%

ARC6 Is a J-Domain Plastid Division Protein and an Evolutionary Descendant of the Cyanobacterial Cell Division Protein Ftn2[W]

et al. 2003

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“…In fact, Hdj1 is even more effective than Hdj2 in refolding luciferase in vitro (54). In general, type I and type II J proteins have a more highly conserved J domain within their own groups and tend to interact with a broader range of substrates, whereas type III J proteins, have a lower level of conservation and a more restricted substrate specificity (55). A broad substrate specificity would be expected if ERdj4 played a role in either the refolding of proteins or the retro-translocation of unfolded proteins during ER stress.…”

Section: Fig 3 Subcellular Localization Of Ha-tagged Erdj4mentioning

confidence: 99%

Identification and Characterization of a Novel Endoplasmic Reticulum (ER) DnaJ Homologue, Which Stimulates ATPase Activity of BiP in Vitro and Is Induced by ER Stress

Shen

Meunier

Hendershot

2002

Journal of Biological Chemistry

190

183

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The activity of Hsp70 proteins is regulated by accessory proteins, which include members of the DnaJ-like protein family. Characterized by the presence of a highly conserved 70-amino acid J domain, DnaJ homologues activate the ATPase activity of Hsp70 proteins and stabilize their interaction with unfolded substrates. DnaJ homologues have been identified in most organelles where they are involved in nearly all aspects of protein synthesis and folding. Within the endoplasmic reticulum (ER), DnaJ homologues have also been shown to assist in the translocation, secretion, retro-translocation, and ER-associated degradation (ERAD) of secretory pathway proteins. By using bioinformatic methods, we identified a novel mammalian DnaJ homologue, ERdj4. It is the first ER-localized type II DnaJ homologue to be reported. The signal sequence of ERdj4 remains uncleaved and serves as a membrane anchor, orienting its J domain into the ER lumen. ERdj4 colocalized with GRP94 in the ER and associated with BiP in vivo when they were co-expressed in COS-1 cells. In vitro experiments demonstrated that the J domain of ERdj4 stimulated the ATPase activity of BiP in a concentration-dependent manner. However, mutation of the hallmark tripeptide HPD (His 3 Gln) in the J domain totally abolished this activation. ERdj4 mRNA expression was detected in all human tissues examined but showed the highest level of the expression in the liver, kidney, and placenta. We found that ERdj4 was highly induced at both the mRNA and protein level in response to ER stress, indicating that this protein might be involved in either protein folding or ER-associated degradation. The endoplasmic reticulum (ER)1 is the site of synthesis and maturation of secretory pathway proteins, which include resident proteins of the endocytic and exocytic organelles as well as surface and secreted proteins. Approximately one-third of all cellular proteins are translocated into the lumen of ER, which possesses a unique oxidizing and Ca 2ϩ -rich environment, where post-translational modification, folding, and oligomerization of nascent proteins occur. ER molecular chaperones and folding enzymes associate with the newly synthesized proteins to prevent their aggregation and help them fold and assemble correctly. Through a process called ER quality control, proteins that do not mature properly are retained in the ER and are eventually targeted for ER-associated degradation (ERAD) through the action of the chaperones (1).BiP, also known as GRP78, is the mammalian ER member of the Hsp70 family and was the first component of the ER quality control apparatus to be identified (2). Hsp70 family members exist in all organisms and in all organelles, where they aid in the folding and assembly of nascent proteins and prevent their aggregation during conditions of physiological stress (3, 4). Like other Hsp70 proteins, BiP plays an essential role in the biosynthesis of proteins. In addition, BiP maintains the permeability barrier of the ER translocon during early stages of protein translocation ...

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“…According to the homology of the DnaJ protein of E.coli, Hsp40 proteins were classified into three types: Type I DnaJ proteins (DnaJA) possess all four parts of DnaJ protein in E. coli; Type II DnaJ proteins (DnaJB) possess the N-terminus Jdomain and the glycine/phenylalanine-rich region; Type III DnaJ proteins (DnaJC) only have a J-domain, which is not necessarily located at N-terminus of the protein [11,12]. Recently, type IV DnaJ protein family was added, which differs from the other three types of DnaJ proteins in that it owns a 'J-like' domain [6,13,14] containing various mutations in a highly conserved histidine, proline, and aspartic acid-HPD motif located between helices II and III in DnaJ domain [6,[15][16][17]. However, Peter Walsh et al (2004) proposed that the term J-proteins should be used more strictly to describe only J proteins with well-conserved Jdomain in the HPD motif, while structurally less-conserved proteins should be referred to as J-like proteins [6].…”

Section: Introductionmentioning

confidence: 99%

Genome-wide identification of Hsp70 genes in channel catfish and their regulated expression after bacterial infection

Song

Xie

et al. 2016

Fish & Shellfish Immunology

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Analysis of the levels of conservation of the J domain among the various types of DnaJ-like proteins

Cited by 79 publications

References 21 publications

ARC6 Is a J-Domain Plastid Division Protein and an Evolutionary Descendant of the Cyanobacterial Cell Division Protein Ftn2[W]

ARC6 Is a J-Domain Plastid Division Protein and an Evolutionary Descendant of the Cyanobacterial Cell Division Protein Ftn2[W]

Identification and Characterization of a Novel Endoplasmic Reticulum (ER) DnaJ Homologue, Which Stimulates ATPase Activity of BiP in Vitro and Is Induced by ER Stress

Genome-wide identification of Hsp70 genes in channel catfish and their regulated expression after bacterial infection

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