skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Extensive amino acid sequence homologies between animal lectins

Abstract

The authors have established the amino acid sequence of the ..beta..-D-galactoside binding lectin from the electric eel and the sequences of several peptides from a similar lectin isolated from human placenta. These sequences were compared with the published sequences of peptides derived from the ..beta..-D-galactoside binding lectin from human lung and with sequences deduced from cDNAs assigned to the ..beta..-D-galactoside binding lectins from chicken embryo skin and human hepatomas. Significant homologies were observed. One of the highly conserved regions that contains a tryptophan residue and two glutamic acid resides is probably part of the ..beta..-D-galactoside binding site, which, on the basis of spectroscopic studies of the electric eel lectin, is expected to contain such residues. The similarity of the hydropathy profiles and the predicted secondary structure of the lectins from chicken skin and electric eel, in spite of differences in their amino acid sequences, strongly suggests that these proteins have maintained structural homologies during evolution and together with the other ..beta..-D-galactoside binding lectins were derived form a common ancestor gene.

Authors:
; ; ;
Publication Date:
Research Org.:
University Paris, VIII (France)
OSTI Identifier:
7000976
Resource Type:
Journal Article
Resource Relation:
Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States); Journal Volume: 84:18
Country of Publication:
United States
Language:
English
Subject:
54 ENVIRONMENTAL SCIENCES; LECTINS; AMINO ACID SEQUENCE; BIOLOGICAL EVOLUTION; CHICKENS; EEL; ELECTROPHORESIS; EMBRYOS; GLUTAMIC ACID; HEPATOMAS; LIQUID COLUMN CHROMATOGRAPHY; MAN; PLACENTA; RECOMBINANT DNA; SKIN; TRYPTOPHAN; AMINO ACIDS; ANIMALS; AQUATIC ORGANISMS; AROMATICS; AZAARENES; AZOLES; BIRDS; BODY; CARBOXYLIC ACIDS; CHROMATOGRAPHY; DISEASES; DNA; FETAL MEMBRANES; FISHES; FOWL; HETEROCYCLIC ACIDS; HETEROCYCLIC COMPOUNDS; INDOLES; MAMMALS; MEMBRANES; MOLECULAR STRUCTURE; NEOPLASMS; NUCLEIC ACIDS; ORGANIC ACIDS; ORGANIC COMPOUNDS; ORGANIC NITROGEN COMPOUNDS; ORGANS; PRIMATES; PYRROLES; SEPARATION PROCESSES; VERTEBRATES; 500200* - Environment, Atmospheric- Chemicals Monitoring & Transport- (-1989)

Citation Formats

Paroutaud, P., Levi, G., Teichberg, V.I., and Strosberg, A.D.. Extensive amino acid sequence homologies between animal lectins. United States: N. p., 1987. Web. doi:10.1073/pnas.84.18.6345.
Paroutaud, P., Levi, G., Teichberg, V.I., & Strosberg, A.D.. Extensive amino acid sequence homologies between animal lectins. United States. doi:10.1073/pnas.84.18.6345.
Paroutaud, P., Levi, G., Teichberg, V.I., and Strosberg, A.D.. Tue . "Extensive amino acid sequence homologies between animal lectins". United States. doi:10.1073/pnas.84.18.6345.
@article{osti_7000976,
title = {Extensive amino acid sequence homologies between animal lectins},
author = {Paroutaud, P. and Levi, G. and Teichberg, V.I. and Strosberg, A.D.},
abstractNote = {The authors have established the amino acid sequence of the ..beta..-D-galactoside binding lectin from the electric eel and the sequences of several peptides from a similar lectin isolated from human placenta. These sequences were compared with the published sequences of peptides derived from the ..beta..-D-galactoside binding lectin from human lung and with sequences deduced from cDNAs assigned to the ..beta..-D-galactoside binding lectins from chicken embryo skin and human hepatomas. Significant homologies were observed. One of the highly conserved regions that contains a tryptophan residue and two glutamic acid resides is probably part of the ..beta..-D-galactoside binding site, which, on the basis of spectroscopic studies of the electric eel lectin, is expected to contain such residues. The similarity of the hydropathy profiles and the predicted secondary structure of the lectins from chicken skin and electric eel, in spite of differences in their amino acid sequences, strongly suggests that these proteins have maintained structural homologies during evolution and together with the other ..beta..-D-galactoside binding lectins were derived form a common ancestor gene.},
doi = {10.1073/pnas.84.18.6345},
journal = {Proc. Natl. Acad. Sci. U.S.A.; (United States)},
number = ,
volume = 84:18,
place = {United States},
year = {Tue Sep 01 00:00:00 EDT 1987},
month = {Tue Sep 01 00:00:00 EDT 1987}
}
  • The complete amino acid sequence for human erythrocyte band 4.2 has been derived from the nucleotide sequence of a full-length 2.35-kilobase (kb) cDNA. The 2.35-kb cDNA was isolated from a human reticulocyte cDNA library made in the expression vector {lambda}gt11. Of the 2348 base pairs (bp), 2073 bp encode 691 amino acids representing 76.9 kDa. RNA blot analysis of human reticulocyte total RNA gives a message size for band 4.2 of 2.4 kb. The amino acid sequence of band 4.2 has homology with two closely related Ca{sup 2+}-dependent crosslinking proteins, guinea pig liver transglutaminase and the a subunit of humanmore » coagulation factor XIII, transglutaminase that forms intermolecular {gamma}-glutamyl-{epsilon}-lysine bonds between fibrin molecules. The region of greatest identity includes a 49-amino acid stretch of band 4.2, which is 69% and 51% identical with guinea pig liver transglutaminase and the a subunit of factor XIII, respectively, within the regions that contain the active sites of these enzymes. Significantly, within the five contiguous consensus residues of the transglutaminase active site, Gly-Gln-Cys-Trp-Val, band 4.2 has an alanine substituted for cysteine. Consistent with this active site substitution, erythrocyte membranes or inside-out vesicles, which contain band 4.2, show no evidence of transglutaminase activity by two types of in vitro assay.« less
  • The authors have purified the human lymphocyte Fc receptor specific for IgE (Fcepsilon receptor) and its soluble form by using the anti-Fcepsilon receptor monoclonal antibody H107. Using an oligonucleotide probe corresponding to the partial amino acid sequence of the soluble Fcepsilon receptor related to IgE binding factor, they cloned, sequenced, and expressed a cDNA for the receptor. The Fcepsilon receptor has 321 amino acid residues with no NH/sub 2/-terminal signal sequence. The receptor was separated into two domains by a putative 24-amino acid residue transmembrane region located near the NH/sub 2/-terminal end. The Fcepsilon receptor showed a marked homology withmore » animal lectins including human and rat asialoglycoprotein receptors, chicken hepatic lectin, and rat mannose binding proteins.« less
  • NAD(P)H:quinone oxidoreductases (NQOs) are flavoproteins that catalyze the oxidation of NADH or NADPH by various quinones and oxidation-reduction dyes. The authors previously described a complementary DNA that encodes a dioxin-inducible cytosolic form of human NAD(P)H:quinone oxidoreductase (NQO{sub 1}). In the present report they describe the nucleotide sequence and deduced amino acid sequence for a cDNA clone that is likely to encode a second form of NAD(P)H:quinone oxidoreductase (NQO{sub 2}) which was isolated by screening a human liver cDNA library by hybridization with a NQO{sub 1} cDNA probe. The NQO{sub 2} cDNA is 976 nucleotides long and encodes a protein ofmore » 231 amino acids. COS1 cells transfected with NQO{sub 2} cDNA showed a 5-7 fold increase in NAD(P)H:quinone oxidoreductase activity as compared to nontransfected cells when either 2,6-dichlorophenolindophenol or menadione was used as substrate. The NQO{sub 2} gene locus is highly polymorphic as indicated by several restriction fragment length polymorphisms detected with five different restriction enzymes. The NQO{sub 2} gene was localized to human chromosome 6 by Southern analysis of human-rodent somatic cell hybrids.« less
  • The complete nucleotide sequence of the gene encoding the surface (hexagonally packed intermediate (HPI))-layer polypeptide of Deinococcus radiodurans Sark was determined and found to encode a polypeptide of 1036 amino acids. Amino acid sequence analysis of about 30% of the residues revealed that the mature polypeptide consists of at least 978 amino acids. The N terminus was blocked to Edman degradation. The results of proteolytic modification of the HPI layer in situ and M/sub r/ estimations of the HPI polypeptide expressed in Escherichia coli indicated that there is a leader sequence. The N-terminal region contained a very high percentage (29%)more » of threonine and serine, including a cluster of nine consecutive serine or threonine residues, whereas a stretch near the C terminus was extremely rich in aromatic amino acids (29%). The protein contained at least two disulfide bridges, as well as tightly bound reducing sugars and fatty acids.« less