Phylogenetic and Primary Sequence Characterization of Cathepsin B Cysteine Proteases from the Oxymonad Flagellate <i>Monocercomonoides</i>

Dacks, Joel B.; Kuru, Teklu; Liapounova, Natalia A.; Gedamu, Lashitew

doi:10.1111/j.1550-7408.2007.00296.x

Cited by 13 publications

(5 citation statements)

References 30 publications

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“…2008) (supplementary table S7, Supplementary Material online). The expansion of cysteine proteases is consistent with the expanded complement of Cathepsin B cysteine proteases previously observed in M. exilis (Dacks et al. 2008).…”

Section: Resultssupporting

confidence: 90%

The Oxymonad Genome Displays Canonical Eukaryotic Complexity in the Absence of a Mitochondrion

Karnkowska

Treitli

Brzoň

et al. 2019

Molecular Biology and Evolution

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The discovery that the protist Monocercomonoides exilis completely lacks mitochondria demonstrates that these organelles are not absolutely essential to eukaryotic cells. However, the degree to which the metabolism and cellular systems of this organism have adapted to the loss of mitochondria is unknown. Here, we report an extensive analysis of the M. exilis genome to address this question. Unexpectedly, we find that M. exilis genome structure and content is similar in complexity to other eukaryotes and less “reduced” than genomes of some other protists from the Metamonada group to which it belongs. Furthermore, the predicted cytoskeletal systems, the organization of endomembrane systems, and biosynthetic pathways also display canonical eukaryotic complexity. The only apparent preadaptation that permitted the loss of mitochondria was the acquisition of the SUF system for Fe–S cluster assembly and the loss of glycine cleavage system. Changes in other systems, including in amino acid metabolism and oxidative stress response, were coincident with the loss of mitochondria but are likely adaptations to the microaerophilic and endobiotic niche rather than the mitochondrial loss per se. Apart from the lack of mitochondria and peroxisomes, we show that M. exilis is a fully elaborated eukaryotic cell that is a promising model system in which eukaryotic cell biology can be investigated in the absence of mitochondria.

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Section: Resultssupporting

confidence: 90%

The Oxymonad Genome Displays Canonical Eukaryotic Complexity in the Absence of a Mitochondrion

Karnkowska

Treitli

Brzoň

et al. 2019

Molecular Biology and Evolution

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“…All animal cathepsin B enzymes, including those from human [18], cattle [19], mouse [18], chicken [20], Atlantic halibut (DDBJ acession number ), yellow mealworm [21] and Clonorchis sinensis (DDBJ accession number ), possess similar occluding loop structures. The occluding loop structure is also conserved in invertebrates; however, the loop is either partially or entirely absent in CBCPs from some parasites and nematodes [22–25]. Two types of CBCP that have a loop containing a dihistidine motif ( Trypanosoma congolense ‐1) or a single histidine ( T. congolense ‐6) were present in Trypanosoma [25], as shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

“…4, sequences within the occluding loop of cathepsin B are highly conserved in vertebrates and invertebrates. However, some parasitic organisms and nematodes possess a modified loop sequence, comprising either amino acid or small peptide inserts or large deletions [23–25]. In contrast, plant CBCP possesses only one histidine within the loop.…”

Section: Discussionmentioning

confidence: 99%

Purification and characterization of cathepsin B‐like cysteine protease from cotyledons of daikon radish, Raphanus sativus

et al. 2008

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Genome analysis has indicated that plants, like animals, possess a variety of protease genes. The Arabidopsis thaliana genome has 680 protease (known and putative peptidase) sequences representing all six catalytic types: aspartic, cysteine, glutamic, metallo, serine and threonine peptidases (MEROPS peptidase database; http://merops.sanger.ac.uk/), reflecting the diverse functions of plant proteases. In A. thaliana, cDNAs encoding 10 members [vignain, brassicain, RD19A, pseudotzain, aleurain Plant cathepsin B-like cysteine protease (CBCP) plays a role in disease resistance and in protein remobilization during germination. The ability of animal cathepsin B to function as a dipeptidyl carboxypeptidase has been attributed to the presence of a dihistidine (His110-His111) motif in the occluding loop, which represents a unique structure of cathepsin B. However, a dihistidine motif is not present in the predicted sequence of the occluding loop of plant CBCP, as determined from cDNA sequence analysis, and the loop is shorter. In an effort to investigate the enzymatic properties of plant CBCP, which possesses the unusual occluding loop, we have purified CBCP from the cotyledons of daikon radish (Raphanus sativus) by chromatography through Sephacryl S-200, DEAE-cellulose, hydroxyapatite and organomercurial-Sepharose. The molecular mass of the enzyme was estimated to be 28 kDa by SDS ⁄ PAGE under reducing conditions. The best synthetic substrate for CBCP was t-butyloxycarbonyl Leu-Arg-Arg-4-methylcoumaryl 7-amide, as is the case with human cathepsin B. However, the endopeptidase activity of CBCP towards glucagon and adrenocorticotropic hormone showed broad cleavage specificity. Human cathepsin B preferentially cleaves model peptides via its dipeptidyl carboxypeptidase activity, whereas daikon CBCP displays both endopeptidase and exopeptidase activities. In addition, CBCP was found to display carboxymonopeptidase activity against the substrate o-aminobenzoyl-Phe-Arg-Phe(4-NO 2 ). Daikon CBCP is less sensitive (1 ⁄ 7000) to CA-074 than human cathepsin B. Expression analysis of CBCP at the protein and RNA levels indicated that daikon CBCP activity in cotyledons is regulated by post-transcriptional events during germination.Abbreviations

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“…In cathepsin L subfamily, the propeptide comprises 100 residues and 2 conserved motifs, namely, ERFNIN and GNFD. In cathepsin B subfamily, the propeptide is approximately 60 residues in length and contains the GNFD motif only 15 - 17 .…”

Section: Introductionmentioning

confidence: 99%

Evolutionary History of Cathepsin L (L-like) Family Genes in Vertebrates

Zhou¹,

Zhang

et al. 2015

Int. J. Biol. Sci.

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Cathepsin L family, an important cysteine protease found in lysosomes, is categorized into cathepsins B, F, H, K, L, S, and W in vertebrates. This categorization is based on their sequence alignment and traditional functional classification, but the evolutionary relationship of family members is unclear. This study determined the evolutionary relationship of cathepsin L family genes in vertebrates through phylogenetic construction. Results showed that cathepsins F, H, S and K, and L and V were chronologically diverged. Tandem-repeat duplication was found to occur in the evolutionary history of cathepsin L family. Cathepsin L in zebrafish, cathepsins S and K in xenopus, and cathepsin L in mice and rats underwent evident tandem-repeat events. Positive selection was detected in cathepsin L-like members in mice and rats, and amino acid sites under positive selection pressure were calculated. Most of these sites appeared at the connection of secondary structures, suggesting that the sites may slightly change spatial structure. Severe positive selection was also observed in cathepsin V (L2) of primates, indicating that this enzyme had some special functions. Our work provided a brief evolutionary history of cathepsin L family and differentiated cathepsins S and K from cathepsin L based on vertebrate appearance. Positive selection was the specific cause of differentiation of cathepsin L family genes, confirming that gene function variation after expansion events was related to interactions with the environment and adaptability.

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Phylogenetic and Primary Sequence Characterization of Cathepsin B Cysteine Proteases from the Oxymonad Flagellate Monocercomonoides

Cited by 13 publications

References 30 publications

The Oxymonad Genome Displays Canonical Eukaryotic Complexity in the Absence of a Mitochondrion

The Oxymonad Genome Displays Canonical Eukaryotic Complexity in the Absence of a Mitochondrion

Purification and characterization of cathepsin B‐like cysteine protease from cotyledons of daikon radish, Raphanus sativus

Evolutionary History of Cathepsin L (L-like) Family Genes in Vertebrates

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