Amino acid sequence of human pregnancy-associated plasma protein A derived from cloned cDNA

Biochemistry ◽  
1994 ◽  
Vol 33 (6) ◽  
pp. 1592-1598 ◽  
Author(s):  
Torsten Kristensen ◽  
Claus Oxvig ◽  
Ole Sand ◽  
Niels Peter Hundahl Moeller ◽  
Lars Sottrup-Jensen
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Plasma Protein ◽  
Protein A ◽  
Human Pregnancy ◽  
Cloned Cdna

scholarly journals Molecular cloning and characterization of the cDNA coding for C4b-binding protein, a regulatory protein of the classical pathway of the human complement system

1985 ◽  
Vol 230 (1) ◽  
pp. 133-141 ◽  
Author(s):  
L P Chung ◽  
D R Bentley ◽  
K B Reid
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cdna Sequence ◽  
Binding Protein ◽  
Regulatory Protein ◽  
Protein A ◽  
Classical Pathway ◽  
Amino Acid Residues ◽  
Cloned Cdna

By using synthetic oligonucleotides as probes, plasmid clones containing portions of cDNA coding for human C4b-binding protein were isolated from a liver cDNA library. The entire amino acid sequence of the C4b-binding protein can be predicted from this study of the cloned cDNA when allied to a previous sequence study at the protein level [Chung, Gagnon & Reid (1985) Mol. Immunol. 22, 427-435], in which over 55% of the amino acid sequence, including the N-terminal 62 residues, was obtained. The plasmid clones isolated allowed the unambiguous determination of 1717 nucleotides of cDNA sequence between the codon for the 32nd amino acid in the sequence of C4b-binding protein and the 164th nucleotide in the 3′ non-translated region. The sequence studies show that the secreted form of C4b-binding protein, found in plasma, is composed of chains of apparent Mr 70 000 that contains 549 amino acid residues. Examination of the protein and cDNA sequence results show that there are at least two polymorphic sites in the molecule. One is at position 44, which can be glutamine or threonine, and the other is at position 309, which can be tyrosine or histidine. Northern-blot analysis indicated that the mRNA for C4b-binding protein is approx. 2.5 kilobases long. The N-terminal 491 amino acids of C4b-binding protein can be divided into eight internal homologous regions, each approx. 60 amino acids long, which can be aligned by the presence in each region of four half-cystine, one tryptophan and several other conserved residues. These regions in C4b-binding protein are homologous with the three internal-homology regions that have been reported to be present within the Ba region of the complement enzyme factor B and also to the internal-homology regions found in the non-complement beta 2-glycoprotein I.

Complete amino acid sequence of the human progesterone receptor deduced from cloned cDNA

1987 ◽  
Vol 143 (2) ◽  
pp. 740-748 ◽  
Author(s):  
Micheline Misrahi ◽  
Michel Atger ◽  
Luc d'Auriol ◽  
Hugues Loosfelt ◽  
Cécile Meriel ◽  
...  
Keyword(s):  
Amino Acid ◽  
Progesterone Receptor ◽  
Amino Acid Sequence ◽  
Complete Amino Acid Sequence ◽  
Cloned Cdna ◽  
Human Progesterone Receptor

scholarly journals Partial sequence of the purified protein confirms the identity of cDNA coding for human lysosomal α-mannosidase B

1995 ◽  
Vol 305 (2) ◽  
pp. 363-366 ◽  
Author(s):  
C Emiliani ◽  
S Martino ◽  
J L Stirling ◽  
B Maras ◽  
A Orlacchio
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Rapid Method ◽  
Protein Sequencing ◽  
Subunit Composition ◽  
Partial Sequence ◽  
Sequencing Analysis ◽  
Cloned Cdna

Human lysosomal alpha-mannosidase has been purified by a simple and rapid method in sufficient quantities for the analysis of its subunit composition and partial protein sequencing. Analysis of the N-terminal residues of the 30 kDa polypeptide has enabled us to confirm the identity of the recently cloned cDNA that was tentatively identified as that of lysosomal alpha-mannosidase [Nebes and Schmidt (1994) Biochem. Biophys. Res. Commun. 200, 239-245] and to locate the position of this polypeptide within the total deduced amino acid sequence. This finding will therefore provide a firm foundation for the characterization of alpha-mannosidosis mutations.

scholarly journals Mutagenesis of the Rns regulator of enterotoxigenic Escherichia coli reveals roles for a linker sequence and two helix–turn–helix motifs

Microbiology ◽  
2010 ◽  
Vol 156 (9) ◽  
pp. 2796-2806 ◽  
Author(s):  
Vivienne Mahon ◽  
Cyril J. Smyth ◽  
Stephen G. J. Smith
Keyword(s):  
Gene Expression ◽  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Protein A ◽  
Diarrhoeal Disease ◽  
Enterotoxigenic Escherichia Coli ◽  
Insertion Mutagenesis

The pathogenesis of diarrhoeal disease due to human enterotoxigenic Escherichia coli absolutely requires the expression of fimbriae. The expression of CS1 fimbriae is positively regulated by the AraC-like protein Rns. AraC-like proteins are DNA-binding proteins that typically contain two helix–turn–helix (HTH) motifs. A program of pentapeptide insertion mutagenesis of the Rns protein was performed, and this revealed that both HTH motifs are required by Rns to positively regulate CS1 fimbrial gene expression. Intriguingly, a pentapeptide insertion after amino acid C102 reduced the ability of Rns to transactivate CS1 fimbrial expression. The structure of Rns in this vicinity (NACRS) was predicted to be disordered and thus might act as a flexible linker. This hypothesis was confirmed by deletion of this amino acid sequence from the Rns protein; a truncated protein that lacked this sequence was no longer functional. Strikingly, this sequence could be functionally substituted in vivo and in vitro by a flexible seven amino acid sequence from another E. coli AraC-like protein RhaS. Our data indicate that HTH motifs and a flexible sequence are required by Rns for maximal activation of fimbrial gene expression.

Amino Acid Sequence of Hen Ovomacroglobulin (Ovostatin) deduced from cloned cDNA

DNA Sequence ◽  
1994 ◽  
Vol 5 (2) ◽  
pp. 111-119 ◽  
Author(s):  
Kåre L. Nielsen ◽  
Lars Sottrup-Jensen ◽  
Hideaki Nagase ◽  
Hans Chr Thøgersen ◽  
Michael Etzerodt
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cloned Cdna
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