Cloning, sequencing and expression of VAT, a CDC48/p97 ATPase homologue from the archaeon <i>Thermoplasma acidophilum</i>

Pamnani, Vashu; Tamura, Tomohiro; Lupas, Andrei N.; Peters, Jürgen; Cejka, Zdenka; Ashraf, William; Baumeister, Wolfgang

doi:10.1016/s0014-5793(97)00138-5

Cited by 62 publications

(41 citation statements)

References 43 publications

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“…12-subunit configuration of PAN suggested that it may associate as two stacked hexameric rings similar to other related ATPases including the mammalian NSF (26), Thermoplasma VAT (48), and Rhodococcus ARC complexes (76). Transmission electron micrographs of the recombinant PAN proteins revealed particles of 10 to 14 nm in diameter which were somewhat ring-like but not distinct hexameric or symmetrical complexes (Fig.…”

Section: Purification Of the Proteasome-activating Nucleotidase (Pan)mentioning

confidence: 80%

Biochemical and Physical Properties of theMethanococcus jannaschii20S Proteasome and PAN, a Homolog of the ATPase (Rpt) Subunits of the Eucaryal 26S Proteasome

Wilson

Aldrich

et al. 2000

J Bacteriol

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The 20S proteasome is a self-compartmentalized protease which degrades unfolded polypeptides and has been purified from eucaryotes, gram-positive actinomycetes, and archaea. Energy-dependent complexes, such as the 19S cap of the eucaryal 26S proteasome, are assumed to be responsible for the recognition and/or unfolding of substrate proteins which are then translocated into the central chamber of the 20S proteasome and hydrolyzed to polypeptide products of 3 to 30 residues. All archaeal genomes which have been sequenced are predicted to encode proteins with up to ϳ50% identity to the six ATPase subunits of the 19S cap. In this study, one of these archaeal homologs which has been named PAN for proteasome-activating nucleotidase was characterized from the hyperthermophile Methanococcus jannaschii. In addition, the M. jannaschii 20S proteasome was purified as a 700-kDa complex by in vitro assembly of the ␣ and ␤ subunits and has an unusually high rate of peptide and unfolded-polypeptide hydrolysis at 100°C. The 550-kDa PAN complex was required for CTP-or ATP-dependent degradation of ␤-casein by archaeal 20S proteasomes. A 500-kDa complex of PAN(⌬1-73), which has a deletion of residues 1 to 73 of the deduced protein and disrupts the predicted N-terminal coiled-coil, also facilitated this energy-dependent proteolysis. However, this deletion increased the types of nucleotides hydrolyzed to include not only ATP and CTP but also ITP, GTP, TTP, and UTP. The temperature optimum for nucleotide ( Energy-dependent proteolysis is not only vital to elimination of defective cellular proteins but is also central to regulation of cell division, metabolism, transcription, and other essential cellular functions (12,22). A small group of related energydependent proteases have been identified from several diverse organisms; these proteases include Lon, FtsH (HflB), ClpAP, ClpXP, HslUV (ClpYQ), and the 26S proteasome (4, 39). Although this group of proteins shares limited primary sequence identity, the proteases have converged to a universal structure in which relatively nonspecific proteolytic active sites are compartmentalized from the cell by narrow openings (37, 67). The current model is that the degradation of biological substrates by this group of proteases requires additional energy-dependent proteins or protein domains for the recognition and/or unfolding of substrate proteins (21,29,65). Some of these energy-dependent components may not only participate in proteolysis but also have independent roles as chaperones (60). Thus, the energy-dependent component of these proteases may provide a proofreading step following the initial binding of protein substrates and enable the cell to distinguish between proteins destined for refolding, disaggregation, or destruction (23).Some energy-dependent proteases are organized in a symmetry mismatch, including ClpAP and ClpXP which are complexes of the hexameric ClpA and ClpX ATPases interfaced with the ClpP protease of two heptameric rings (5). It is postulated that hydrolysis of nucleotides...

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Section: Purification Of the Proteasome-activating Nucleotidase (Pan)mentioning

confidence: 80%

Biochemical and Physical Properties of theMethanococcus jannaschii20S Proteasome and PAN, a Homolog of the ATPase (Rpt) Subunits of the Eucaryal 26S Proteasome

Wilson

Aldrich

et al. 2000

J Bacteriol

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“…For the remaining proteases, some ORFs exhibit nonrandom distribution among representative strains. Of interest, vat.2, encoding hemoglobin protease (55), is present in all strains in group 1 but absent from group 2 strains (Table 5). Similarly, yeaZ, encoding a putative glycoprotein endopeptidase, is absent only in group 2 strains EC10 and RS168 (Table 5).…”

Section: Resultsmentioning

confidence: 99%

Genomic Comparison of Escherichia coli K1 Strains Isolated from the Cerebrospinal Fluid of Patients with Meningitis

2006

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Escherichia coli is a major cause of enteric/diarrheal diseases, urinary tract infections, and sepsis. E. coli K1 is the leading gram-negative organism causing neonatal meningitis, but the microbial basis of E. coli K1 meningitis is incompletely understood. Here we employed comparative genomic hybridization to investigate 11 strains of E. coli K1 isolated from the cerebrospinal fluid (CSF) of patients with meningitis. These 11 strains cover the majority of common O serotypes in E. coli K1 isolates from CSF. Our data demonstrated that these 11 strains of E. coli K1 can be categorized into two groups based on their profile for putative virulence factors, lipoproteins, proteases, and outer membrane proteins. Of interest, we showed that some open reading frames (ORFs) encoding the type III secretion system apparatus were found in group 2 strains but not in group 1 strains, while ORFs encoding the general secretory pathway are predominant in group 1 strains. These findings suggest that E. coli K1 strains isolated from CSF can be divided into two groups and these two groups of E. coli K1 may utilize different mechanisms to induce meningitis.The mortality and morbidity associated with neonatal gramnegative bacillary meningitis remain significant despite advances in antimicrobial chemotherapy and supportive care. The mortality rates have ranged between 5 and 50%, with the majority (30 to 50%) of surviving infants manifesting neurological sequelae (15, 25). A major contributing factor is the incomplete understanding of the pathogenesis of this disease.Escherichia coli is the most common gram-negative organism that causes meningitis during the neonatal period, and E. coli strains possessing the K1 capsular polysaccharide are predominant (ϳ80%) among isolates from neonatal E. coli meningitis (26,44,58). At present, a few E. coli K1 strains isolated from cerebrospinal fluid (CSF) have been used to study the microbial basis of meningitis, but it is unclear whether the information derived from these E. coli K1 strains is relevant to other E. coli K1 strains isolated from CSF. For example, CNF1 (cytotoxic necrotizing factor 1) and IbeA have been shown to contribute to the pathogenesis of meningitis in strain RS218, i.e., invasion of human brain microvascular endothelial cells (HBMEC) in vitro and traversal of the blood-brain barrier (BBB) in vivo (35, 40), but it is unknown whether CNF1 and IbeA exist and play the same roles in other E. coli K1 strains isolated from CSF. Therefore, a better knowledge of the distribution pattern of known and putative virulence factors will improve our understanding of meningitis caused by E. coli K1.The distribution of some known E. coli virulence factors has been reported in avian-pathogenic E. coli (APEC) (37), uropathogenic E. coli (21), enteropathogenic E. coli (EPEC), and enterohemorrhagic E. coli (EHEC) (50). For example, the distribution of these known and putative virulence factors has been used to determine phylogenetic relationships among meningitis-causing E. coli isolates (7, 39, 43...

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“…Although many molecular details of ERAD remain unknown, recent work has identified valosin-containing protein (VCP) as a crucial cytoplasmic component of the process (Ye et al, 2001;Bays et al, 2001;Braun et al, 2002;Rabinovich et al, 2002;Jarosch et al, 2002). VCP is a widely distributed AAA ATPase also known as p97 in mammals and amphibians (Peters et al, 1990), TER94 in insects (Pinter et al, 1998), cdc48 in yeast (Moir et al, 1982;Frohlich et al, 1991) and VAT in Archaea (Pamnani et al, 1997). VCP is a ring-shaped homohexamer of a 97 kDa protein that contains two copies of the conserved ATP-binding domain characteristic of AAA family members and an N-terminal polyubiquitin-binding domain (Peters et al, 1990;Dai and Li, 2001).…”

mentioning

confidence: 99%

RNA interference of valosin-containing protein (VCP/p97) reveals multiple cellular roles linked to ubiquitin/proteasome-dependent proteolysis

Wójcik

Yano

DeMartino³

2004

Journal of Cell Science

230

178

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We have used RNA interference (RNAi) to examine the functional relationship between valosin-containing protein (VCP/p97/Cdc48p/TER94) ATPase and the ubiquitin-proteasome system (UPS) in Drosophila S2 and human HeLa cells. In both cell types, RNAi of VCP (and, to a lesser extent, of certain VCP-interacting proteins) caused significant accumulation of high-molecular-weight conjugates of ubiquitin, an indication of inhibited UPS function. However, decreased VCP levels did not directly inhibit proteasome activity. In HeLa cells, polyubiquitinated proteins accumulated as dispersed aggregates rather than as single aggresomes, even in the presence of proteasome inhibitors, which normally promote aggresome formation. RNAi of VCP caused extensive vacuolization of the cytoplasm, and proteasome inhibitors exaggerated this feature. RNAi of VCP had little effect on S2 cell proliferation but blocked cell-cycle progression and induced mitotic abnormalities and apoptosis in HeLa cells. These results indicate that VCP plays an important general role in mediating the function of the UPS, probably by interacting with potential proteasome substrates before they are degraded by the proteasome.

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Cloning, sequencing and expression of VAT, a CDC48/p97 ATPase homologue from the archaeon Thermoplasma acidophilum

Cited by 62 publications

References 43 publications

Biochemical and Physical Properties of theMethanococcus jannaschii20S Proteasome and PAN, a Homolog of the ATPase (Rpt) Subunits of the Eucaryal 26S Proteasome

Biochemical and Physical Properties of theMethanococcus jannaschii20S Proteasome and PAN, a Homolog of the ATPase (Rpt) Subunits of the Eucaryal 26S Proteasome

Genomic Comparison of Escherichia coli K1 Strains Isolated from the Cerebrospinal Fluid of Patients with Meningitis

RNA interference of valosin-containing protein (VCP/p97) reveals multiple cellular roles linked to ubiquitin/proteasome-dependent proteolysis

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