A subtilisin-like serine protease is required for epidermal surface formation inArabidopsisembryos and juvenile plants

Development ◽  
2001 ◽  
Vol 128 (23) ◽  
pp. 4681-4689 ◽  
Author(s):  
Hirokazu Tanaka ◽  
Hitoshi Onouchi ◽  
Maki Kondo ◽  
Ikuko Hara-Nishimura ◽  
Mikio Nishimura ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Serine Proteases ◽  
Land Plants ◽  
Young Embryo ◽  
Epidermal Surface ◽  
Putative Protease ◽  
Excessive Water ◽  
Juvenile Plants

The surfaces of land plants are covered with a cuticle that is essential for retention of water. Epidermal surfaces of Arabidopsis thaliana embryos and juvenile plants that were homozygous for abnormal leaf shape1 (ale1) mutations were defective, resulting in excessive water loss and organ fusion in young plants. In ale1 embryos, the cuticle was rudimentary and remnants of the endosperm remained attached to developing embryos. Juvenile plants had a similar abnormal cuticle. The ALE1 gene was isolated using a transposon-tagged allele ale1-1. The predicted ALE1 amino acid sequence was homologous to those of subtilisin-like serine proteases. The ALE1 gene was found to be expressed within certain endosperm cells adjacent to the embryo and within the young embryo. Expression was not detected after germination. Our results suggest that the putative protease ALE1 affects the formation of cuticle on embryos and juvenile plants and that an appropriate cuticle is required for separation of the endosperm from the embryo and for prevention of organ fusion.

scholarly journals Analysis of Htra Gene from Zebrafish (Danio Rerio)

2015 ◽  
Vol 10 (2) ◽  
Author(s):  
M. Murwantoko ◽  
Chio Oka ◽  
Masashi Kawaichi
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Danio Rerio ◽  
Serine Proteases ◽  
Catalytic Domain ◽  
Fruit Fly ◽  
Wide Range ◽  
Igf Binding ◽  
Bacterial Homolog

HtrA which is characterized by the combination of a trypsin-like catalytic domain with at least one C-terminalPDZ domain is a highly conserved family of serine proteases found in a wide range of organisms. However theidentified HtrA family numbers varies among spesies, for example the number of mammalian, Eschericia coli,fruit fly-HtrA family are 4, 3 and 1 gene respectively. One gene is predicted exist in zebrafish. Since no completeinformation available on zebrafish HtrA, in this paper zebrafish HtrA (zHtrA) gene was analyzed. The zHtrA isbelonged to HtrA1 member and predicted encodes 478 amino acids with a signal peptide, a IGF binding domain,a Kazal-type inhibitor domain in the up stream of HtrA-bacterial homolog. At the amino acid sequence the zHtrA1showed the 69%, 69%, 68%, 54% and 54% with the rat HtrA1, mouse HtrA1, human HtrA1, human HtrA3 andmouse HtrA4 respectively. The zHtrA1 is firstly expressed at 60 hpf and mainly in the vertebral rudiments in thetail region.

Determination of Factor Xa Activity by Means of Chromogenic Substrates Based on the Primary Structure of Prothrombin

1975 ◽  
Author(s):  
L. Aurell ◽  
A. Olausson ◽  
G. Claeson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Primary Structure ◽  
Serine Proteases ◽  
Factor Xa ◽  
Amino Acid Sequences ◽  
Peptide Substrate ◽  
Chromogenic Substrates ◽  
Special Regard

Through the work of Magnusson and co-workers leading to the elucidation of the primary structure of prothrombin including the amino acid sequences around the two bonds split by factor Xa it has been possible to design a synthetic chromogenic peptide substrate. Bz-Ile-Glu-Gly-Arg-pNA, specifically intended for the determination of factor Xa. Furthermore, additional substrates have been synthezised with various alterations in the amino acid sequence. The activity of factor Xa and other serine proteases within the coagulation and fibrinolytic systems towards these substrates will be discussed with special regard to their possible use in coagulation studies.

scholarly journals Protease B of the lysosomelike vacuole of the yeast Saccharomyces cerevisiae is homologous to the subtilisin family of serine proteases.

1987 ◽  
Vol 7 (12) ◽  
pp. 4390-4399 ◽  
Author(s):  
C M Moehle ◽  
R Tizard ◽  
S K Lemmon ◽  
J Smart ◽  
E W Jones
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Serine Proteases ◽  
Proteinase K ◽  
Yeast Saccharomyces Cerevisiae ◽  
Amino Terminal ◽  
Protease B ◽  
Mature Protease

The PRB1 gene of Saccharomyces cerevisiae encodes the vacuolar endoprotease protease B. We have determined the DNA sequence of the PRB1 gene and the amino acid sequence of the amino terminus of mature protease B. The deduced amino acid sequence of this serine protease shares extensive homology with those of subtilisin, proteinase K, and related proteases. The open reading frame of PRB1 consists of 635 codons and, therefore, encodes a very large protein (molecular weight, greater than 69,000) relative to the observed size of mature protease B (molecular weight, 33,000). Examination of the gene sequence, the determined amino-terminal sequence, and empirical molecular weight determinations suggests that the preproenzyme must be processed at both amino and carboxy termini and that asparagine-linked glycosylation occurs at an unusual tripeptide acceptor sequence.

scholarly journals Molecular and immunological characterization and IgE epitope mapping of Pen n 18, a major allergen of Penicillium notatum

2002 ◽  
Vol 363 (3) ◽  
pp. 707-715 ◽  
Author(s):  
Chia-Jung YU ◽  
Yen-Ming CHEN ◽  
Song-Nan SU ◽  
Farhad FOROUHAR ◽  
Shu-Hua LEE ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Serine Proteases ◽  
Major Allergen ◽  
Penicillium Notatum ◽  
Ige Binding ◽  
Acid Protein ◽  
Binding Epitope ◽  
Cross Inhibition ◽  
Amino Acid Protein

The mould genus, Penicillium, is a significant source of environmental aero-allergens. A major allergen from Penicillium notatum, Pen n 18, was identified by two-dimensional immunoblotting using monoclonal antibody G11A10, raised against the vacuolar serine protease of Penicillium citrinum, followed by matrix-assisted laser-desorption ionization—time-of-flight MS analysis of the peptide digest. Pen n 18 was then cloned and the amino acid sequence deduced from the cDNA sequence. The cDNA encoded a 494 amino acid protein, considerably larger than mature Pen n 18, the differences being due to the N- and C-terminal prosequences. The deduced amino acid sequence showed extensive similarity with those of vacuolar serine proteases from various fungi. The Pen n 18 coding sequence was expressed in Escherichia coli as a His-tagged fusion protein and purified by Ni2+-chelate affinity chromatography. On immunoblots, the purified recombinant protein specifically bound IgE from mould-allergic patients, and cross-inhibition assays demonstrated the presence of common IgE-binding epitopes on Pen n 18 and a major allergen of P. citrinum, Pen c 18. When mapping of the allergenic epitopes was performed, at least nine different linear IgE-binding epitopes, located throughout the Pen n 18 protein, were identified. Of these, peptide C12, located in the N-terminal region of the molecule, was recognized by serum from 75% of the patients tested and therefore appears to be an immunodominant IgE-binding epitope.

scholarly journals Cloning cDNAs for Genes Preferentially Expressed during Fruit Growth in Cucumber

1999 ◽  
Vol 124 (2) ◽  
pp. 136-139 ◽  
Author(s):  
Takuro Suyama ◽  
Kunio Yamada ◽  
Hitoshi Mori ◽  
Kiyotoshi Takeno ◽  
Shohei Yamaki
Keyword(s):  
Arabidopsis Thaliana ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Ribosomal Protein ◽  
Time Course ◽  
Large Subunit ◽  
Fruit Growth ◽  
Cdna Clones ◽  
Subtraction Hybridization ◽  
Ribosomal Protein L3

A cDNA library was constructed from poly(A)+RNA extracted from pollinated fruit of `PMR-142' cucumber (Cucumis sativus L.). Subtraction hybridization was made between the cDNAs and poly(A)+RNA from unpollinated fruit to isolate cDNA clones that corresponded to the genes preferentially expressed in the pollinated fruit. We isolated three cDNAs, which were 756, 826, and 998 nucleotides long and designated Csf1, Csf2, and Csf3, respectively. When fruit growth was triggered by pollination, auxin treatment and natural parthenocarpy, Csf2 was always expressed. Time course of expression of the Csf2 gene was nearly parallel to that of the fruit growth. Nucleotide sequences of the Csf cDNAs were fully determined. Homology of the deduced amino acid sequence for Csf1 showed 75% identity with a pea extensin. Only 37%, 33%, and 26% homology was found between Csf2 and bell pepper CaSn-2, tobacco FB7-4, and opium poppy gMLP15, respectively. The Csf3 sequence showed 68% identity with the large subunit of 60S ribosomal protein L3 of Arabidopsis thaliana.

scholarly journals Identification and in silico structural and functional analysis of a trypsin-like protease from shrimp Macrobrachium carcinus

PeerJ ◽  
2020 ◽  
Vol 8 ◽  
pp. e9030 ◽  
Author(s):  
José M. Viader-Salvadó ◽  
José Alberto Aguilar Briseño ◽  
Juan A. Gallegos-López ◽  
José A. Fuentes-Garibay ◽  
Carlos Alfonso Alvarez-González ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Serine Proteases ◽  
Macrobrachium Rosenbergii ◽  
Catalytic Triad ◽  
Activation Mechanism ◽  
Collagenolytic Activity ◽  
Sequence Motif ◽  
Bioinformatics Analyses ◽  
Race Technique

Macrobrachium carcinus (Linnaeus, 1758) is a species of freshwater shrimp widely distributed from Florida southwards to southern Brazil, including southeast of Mexico. In the present work, we identified a putative trypsin-like protease cDNA fragment of 736 nucleotides from M. carcinus hepatopancreas tissue by the 3′RACE technique and compared the deduced amino acid sequence to other trypsin-related proteases to describe its structure and function relationship. The bioinformatics analyses showed that the deduced amino acid sequence likely corresponds to a trypsin-like protease closely related to brachyurins, which comprise a subset of serine proteases with collagenolytic activity found in crabs and other crustacea. The M. carcinus trypsin-like protease sequence showed a global sequence identity of 94% with an unpublished trypsin from Macrobrachium rosenbergii (GenBank accession no. AMQ98968), and only 57% with Penaeus vannamei trypsin (GenBank accession no. CAA60129). A detailed analysis of the amino acid sequence revealed specific differences with crustacean trypsins, such as the sequence motif at the beginning of the mature protein, activation mechanism of the corresponding zymogen, amino acid residues of the catalytic triad and residues responsible for substrate specificity.

Amino acid sequence of rat submaxillary tonin reveals similarities to serine proteases

Nature ◽  
1984 ◽  
Vol 307 (5951) ◽  
pp. 555-558 ◽  
Author(s):  
Claude Lazure ◽  
Richard Leduc ◽  
Nabil G. Seidah ◽  
Gaétan Thibault ◽  
Jacques Genest ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Serine Proteases

The complete amino acid sequence of rat submaxillary gland tonin does contain the aspartic acid at the active site: confirmation by protein sequence analyses

1987 ◽  
Vol 65 (4) ◽  
pp. 321-337 ◽  
Author(s):  
C. Lazure ◽  
R. Leduc ◽  
N. G. Seidah ◽  
G. Thibault ◽  
J. Genest ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Active Site ◽  
Serine Proteases ◽  
Submaxillary Gland ◽  
Catalytic Triad ◽  
Complete Amino Acid Sequence ◽  
Molecular Weights ◽  
Amino Acid Peptide ◽  
Close Relationship

The revised amino acid sequence of rat submaxillary gland tonin, a serine protease, does contain the active site Asp residue. The active site of this kallikrein-related enzyme is thus made up of the same catalytic triad (Asp, Ser, and His) found in all known serine proteases. The important Asp residue has now been localized in a 16 amino acid peptide previously reported as missing in the tonin sequence. The complete amino acid sequence thus contains 235 residues corresponding to a molecular weight of 25 658, more in agreement with previously reported molecular weights. Moreover, the revised structure led (a) to the assignment of Arg, Asn, and Val residues instead of His, Asp, and Gly at positions 63, 165, and 169, respectively; (b) to the assignment of residues occupying an overlapping sequence at positions 165–171, and finally (c) to the localization of two N-glycosylation sites at positions 82 and 165. These results further document the close relationship of tonin to the ever expanding kallikrein family.

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