The nucleotide sequence of the yeastPHO5gene: a putative precursor of repressible acid phosphatase contains a signal peptide
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The nucleotide sequence of the PHO5 gene of the yeast, Saccharomyces cerevisiae, which encodes repressible acid phosphatase (APase) was determined. Comparison of N-terminal amino acid sequence deduced from the nucleotide sequence with that of the purified repressible APase revealed the existence of a putative signal peptide in the precursor protein. The signal peptide was shown to contain 17 amino acid residues and its structural features were quite similar to those of higher eukaryotic and prokaryotic signal peptides. The nucleotide sequence of 5' and 3' noncoding flanking regions of the PHO5 gene are also discussed.Cite
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ABSTRACT A novel acid phosphatase containing phosphotyrosyl phosphatase (PTPase) activity, designated PiACP, from Prevotella intermedia ATCC 25611, an anaerobe implicated in progressive periodontal disease, has been purified and characterized. PiACP, a monomer with an apparent molecular mass of 30 kDa, did not require divalent metal cations for activity and was sensitive to orthovanadate but highly resistant to okadaic acid. The enzyme exhibited substantial activity against tyrosine phosphate-containing peptides derived from the epidermal growth factor receptor. On the basis of N-terminal and internal amino acid sequences of purified PiACP, the gene coding for PiACP was isolated and sequenced. The PiACP gene consisted of 792 bp and coded for a basic protein with an M r of 29,164. The deduced amino acid sequence exhibited striking similarity (25 to 64%) to those of members of class A bacterial acid phosphatases, including PhoC of Morganella morganii , and involved a conserved phosphatase sequence motif that is shared among several lipid phosphatases and the mammalian glucose-6-phosphatases. The highly conservative motif HCXAGXXR in the active domain of PTPase was not found in PiACP. Mutagenesis of recombinant PiACP showed that His-170 and His-209 were essential for activity. Thus, the class A bacterial acid phosphatases including PiACP may function as atypical PTPases, the biological functions of which remain to be determined.
DUSP6
Prevotella intermedia
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Two cDNA clones encoding prepro-sphingolipid activator protein 1 (SAP-1) were isolated from a lambda gt11 human hepatoma expression library using polyclonal antibodies. These had inserts of approximately 2 kilobases (lambda-S-1.2 and lambda-S-1.3) and both were both homologous with a previously isolated clone (lambda-S-1.1) for mature SAP-1. We report here the nucleotide sequence of the longer two EcoRI fragments of S-1.2 and S-1.3 that were not the same and the derived amino acid sequences of mature SAP-1 and its prepro form. The open reading frame encodes 19 amino acids, which are colinear with the amino-terminal sequence of mature SAP-1, and extends far beyond the predicted carboxyl terminus of mature SAP-1, indicating extensive carboxyl-terminal processing. The nucleotide sequence of cDNA encoding prepro-SAP-1 includes 1449 bases from the assigned initiation codon ATG at base-pair 472 to the stop codon TGA at base-pair 1921. The first 23 amino acids coded after the initiation ATG are characteristic of a signal peptide. The calculated molecular mass for a polypeptide encoded by 1449 bases is approximately 53 kDa, in keeping with the reported value for pro-SAP-1. The data indicate that after removal of the signal peptide (23 amino acids) mature SAP-1 (78 amino acids) is generated by removing an additional 7 amino acids from the amino terminus and approximately 373 amino acids from the carboxyl terminus. One potential glycosylation site was previously found in mature SAP-1. Three additional potential glycosylation sites are present in the processed carboxyl-terminal polypeptide, which we designate as P-2. The molecular mass of glycosylated pro-SAP-1 is estimated at approximately 69 kDa, assuming glycosylation of all four sites. The value is close to the reported 70-kDa value for glycosylated pro-SAP-1. A computer search failed to reveal homology between P-2 and the sequence of any other protein; its function is uncertain. The 3' untranslated region is composed of 90 base pairs and is incomplete, since it does not contain a polyadenylylation site or a poly(A) tail.
Stop codon
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The properties of three phosphatases from Salmonella typhimurium have been examined. A cyclic 2',3'-nucleotide phosphodiesterase (EC 3.1.4.d) hydrolyzes cyclic 2',3'-purine and -pyrimidine nucleotides, as well as 3'-mononucleotides, and has a pH optimum of about 7.5. It requires divalent cations for activity and has a molecular weight of 67,000. Acid hexose phosphatase (EC 3.1.2.2) possesses activity towards hexose phosphates as well as other sugar phosphates. The enzyme is apparently a dimer of 37,000-dalton subunits. Nonspecific acid phosphatase (EC 3.1.3.2) hydrolyzes a variety of phosphate esters, including nucleotides and sugar phosphates. The enzyme also hydrolyzes the phosphoric anhydride bonds of pyrophosphate and nucleotides. Michaelis constants of the nonspecific acid phosphatase for several of its substrates are in the 1 to 2 mM range. Nonspecific acid phosphatase is a dimer of 27,000-dalton subunits.
Sugar phosphates
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According to the sequence J04601 in Genebank,the primers were designed and flitrated.The Hubei White swine pepsinogen A cDNA was cloned by RT-PCR,which were 1 227bp in length(submitted in Genebank,the accession number is EF108301.),including a ORF(1 158bp),encoding 385 amino acids.The NH2-terminal region present a signal peptide consisted of fifteen amino acids,there are 370 amino acids in the mature protein.In the mature-protein regions,EF108301 sshowed 99.3% and 98.7% identical nucleotide and amino acid residues with J04601.PredictProtein analysis shows that the alteration of nucleotide and amino acid did not change the secondary structure and of the protein.The analysis of codon usage and mRNA secondary structure was benefited for the further research on the choice of vector,host and,the reconstruct of gene.
Cloning (programming)
Protein sequencing
White (mutation)
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Prostatic acid phosphatase
Protein primary structure
Northern blot
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The structure gene of the colonization factor antigen 1 (CFA/1) has been sequenced. The amino acid sequence of CFA/1 precursor deduced from the nucleotide sequence is composed of 170 amino acids. The first 23 amino acids are considered to be the signal peptide of the CFA/1 protein. On the basis of the nucleotide sequence, three amino acids are different from the protein sequence. Amino acid residues at positions 37, 76 and 97 are found to be Ala, Asp and Ser, instead of Val, Asn and Ala as determined by amino acid sequencing. The CFA/1 is very hydrophobic amino acids. Among the total 170 amino acids, 47% of them are hydrophobic amino acids. CFA/1 gene has a typical Shine-Dalgarno sequence and-10 sequence, but no 35 promoter sequence could be found. The G + C ratio of CFA/1 gene is 40%. Observation of negatively stained preparations of the culture with electron microscopy showed that no fimbriae were found on E. coli C600 strain itself, but the cell carrying the plasmid showed thick pili on its surface.
clone (Java method)
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Protein primary structure
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Secretory protein
Signal peptidase
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