Amino acid sequence of the N-terminal domain of yam (Dioscorea japonica) aerial tuber acidic chitinase. Evidence for the presence of a wheat germ agglutinin domain in matured acidic chitinase from unstressed tuber

1992 ◽  
Vol 19 (2) ◽  
pp. 351-354 ◽  
Author(s):  
Tomohiro Araki ◽  
Jiro Funatsu ◽  
Mayumi Kuramoto ◽  
Takao Torikata
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Terminal Domain ◽  
Dioscorea Japonica ◽  
Aerial Tuber

Partial amino acid sequence of the wheat germ Ec protein. Comparison with another protein very rich in half-cystine and glycine: wheat germ agglutinin

1984 ◽  
Vol 62 (9) ◽  
pp. 908-913 ◽  
Author(s):  
Theo Hofmann ◽  
David I. C. Kells ◽  
Byron G. Lane
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Wheat Germ Agglutinin ◽  
High Speed ◽  
Wheat Germ ◽  
Sodium Dodecyl ◽  
Sedimentation Equilibrium ◽  
Partial Sequence ◽  
Edman Degradation

A wheat germ protein (Ec), the dominant site of cysteine incorporation during early (E) germination of isolated wheat embryos, has been partially sequenced by automated Edman degradation. The sequence of residues 1–59 is not significantly similar to the amino acid sequence known for any other protein, including wheat germ agglutinin which, like Ec, is very rich in half-cystine and glycine. The partial sequence for Ec contains an almost identical pattern of half-cystine residues in segments 6–20 and 35–48, a duplication which includes 10 of the 12 half-cystine residues in the sequence. The partial sequence of Ec may include a large part of the complete sequence, but this remains uncertain because it has not been possible to arrive at a definitve estimate of molecular weight using different physical techniques. Protein Ec can be prepared from a reticulocyte lysate in which cell-free synthesis is programmed by bulk wheat germ mRNA. Determination of the distribution of half-cystine moieties between residues 1 and 20 by Edman degradation of the [35S]cysteine-labeled product of cell-free synthesis shows that it is devoid of an N-terminal extension. Unlike wheat germ agglutinin, Ec does not seem to arise by processing of a conspicuously larger precursor protein. Unlike Ec, another wheat germ protein, Em, the most conspicuous methionine-labeled protein when cell-free protein synthesis is directed by wheat germ mRNA, is refractory to direct sequence analysis by Edman degradation. However, again unlike Ec, uncertainty about the molecular weight of Em, based on its mobility in different sodium dodecyl sulphate – polyacrylamide gel systems, has been resolved by virtue of Em being ideally suited to study by the Yphantis high-speed sedimentation equilibrium method.

scholarly journals The Amino Acid Sequence of Wheat Germ Cytochrome c

1967 ◽  
Vol 242 (11) ◽  
pp. 2764-2779
Author(s):  
Frits C. Stevens ◽  
A.N. Glazer ◽  
Emil L. Smith
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Wheat Germ

Association of the brain anion exchanger, AE3, with the repeat domain of ankyrin

1993 ◽  
Vol 105 (4) ◽  
pp. 1137-1142 ◽  
Author(s):  
C.W. Morgans ◽  
R.R. Kopito
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Anion Exchanger ◽  
Deletion Mutant ◽  
Tandem Repeats ◽  
Structural Homology ◽  
Terminal Domain ◽  
Repeat Domain ◽  
The Brain

The 89 kDa NH2-terminal domain of erythrocyte ankyrin is composed almost entirely of 22 tandem repeats of a 33 amino acid sequence and constitutes the binding site for the cytoplasmic NH2-terminal domain of the erythrocyte anion exchanger, AE1. We have developed an assay to evaluate the in vivo interaction between a fragment of ankyrin corresponding to this domain (ANK90) and two non-erythroid anion exchangers, AE2 and AE3, that share considerable structural homology with AE1. Association was assessed by co-immunoprecipitation of ANK90-anion exchanger complexes from detergent extracts of cells cotransfected with plasmids encoding the ankyrin fragment and the anion exchanger or mutants thereof. ANK90 was co-immunoprecipitated with AE1 but not with an AE1 deletion mutant lacking the cytoplasmic NH2-terminal domain. Using this assay, we show that the brain anion exchanger AE3, but not the closely related homologue, AE2, is capable of binding to ankyrin.

scholarly journals Molecular Evolution of the H-NS Protein: Interaction with Hha-Like Proteins Is Restricted to Enterobacteriaceae

2006 ◽  
Vol 189 (1) ◽  
pp. 265-268 ◽  
Author(s):  
Cristina Madrid ◽  
Jesús García ◽  
Miquel Pons ◽  
Antonio Juárez
Keyword(s):  
Amino Acid ◽  
Molecular Evolution ◽  
Amino Acid Sequence ◽  
Protein Interaction ◽  
Terminal Domain ◽  
Key Residues

ABSTRACT We show here that chromosomal hha-like genes are restricted to the Enterobacteriaceae. The H-NS N-terminal domain of members of this family includes an unaltered seven-amino-acid sequence located between helixes 1 and 2, termed the Hha signature, that contains key residues for H-NS-Hha interaction.

scholarly journals Comparison of Amino Acid Sequence of the C-Terminal Domain of Insulin-Responsive Glucose Transporter (GLUT4) in Livestock Mammals.

1998 ◽  
Vol 60 (6) ◽  
pp. 769-771 ◽  
Author(s):  
Hiroyuki ABE ◽  
Yumi KAWAKITA ◽  
Toshikazu MIYASHIGE ◽  
Masami MORIMATSU ◽  
Masayuki SAITO
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Glucose Transporter ◽  
Terminal Domain ◽  
Glucose Transporter Glut4

The wheat-germ Ec protein is a zinc-containing metallothionein

1987 ◽  
Vol 65 (11) ◽  
pp. 1001-1005 ◽  
Author(s):  
Byron Lane ◽  
Robert Kajioka ◽  
Theresa Kennedy
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Experimental Evidence ◽  
Biomedical Research ◽  
Wheat Germ ◽  
Visual Inspection ◽  
Higher Plants ◽  
Washington Dc ◽  
Significant Relation ◽  
Partial Amino Acid Sequence

The partial amino-acid sequence of the wheat-germ Ec protein has been published previously. Computer analysis failed to show a significant relation between the amino-acid sequence of Ec and the sequences of other proteins stored in the data base of the National Biomedical Research Foundation, Washington, DC. Visual inspection and comparison of the amino-acid sequence of Ec with the sequences of other proteins rich in half-cystine have revealed that the amino-acid sequence of Ec bears a compelling relation to sequences reported for animal metallothioneins. Experimental evidence is presented which supports the view that Ec is a zinc-containing metallothionein, the first metallothionein from higher plants for which an almost complete amino-acid sequence has been determined.

scholarly journals Molecular Characterization of a Novel Glucosyltransferase from Lactobacillus reuteri Strain 121 Synthesizing a Unique, Highly Branched Glucan with α-(1→4) and α-(1→6) Glucosidic Bonds

2002 ◽  
Vol 68 (9) ◽  
pp. 4283-4291 ◽  
Author(s):  
S. Kralj ◽  
G. H. van Geel-Schutten ◽  
H. Rahaoui ◽  
R. J. Leer ◽  
E. J. Faber ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Molecular Characterization ◽  
Lactobacillus Reuteri ◽  
Degenerate Primers ◽  
Terminal Domain ◽  
Branching Points ◽  
Culture Supernatants

ABSTRACT Lactobacillus reuteri strain 121 produces a unique, highly branched, soluble glucan in which the majority of the linkages are of the α-(1→4) glucosidic type. The glucan also contains α-(1→6)-linked glucosyl units and 4,6-disubstituted α-glucosyl units at the branching points. Using degenerate primers, based on the amino acid sequences of conserved regions from known glucosyltransferase (gtf) genes from lactic acid bacteria, the L. reuteri strain 121 glucosyltransferase gene (gtfA) was isolated. The gtfA open reading frame (ORF) was 5,343 bp, and it encodes a protein of 1,781 amino acids with a deduced M r of 198,637. The deduced amino acid sequence of GTFA revealed clear similarities with other glucosyltransferases. GTFA has a relatively large variable N-terminal domain (702 amino acids) with five unique repeats and a relatively short C-terminal domain (267 amino acids). The gtfA gene was expressed in Escherichia coli, yielding an active GTFA enzyme. With respect to binding type and size distribution, the recombinant GTFA enzyme and the L. reuteri strain 121 culture supernatants synthesized identical glucan polymers. Furthermore, the deduced amino acid sequence of the gtfA ORF and the N-terminal amino acid sequence of the glucosyltransferase isolated from culture supernatants of L. reuteri strain 121 were the same. GTFA is thus responsible for the synthesis of the unique glucan polymer in L. reuteri strain 121. This is the first report on the molecular characterization of a glucosyltransferase from a Lactobacillus strain.

Amino acid sequence of the N-terminal domain of calf thymus histone H2A.Z

FEBS Letters ◽  
1983 ◽  
Vol 154 (1) ◽  
pp. 166-170 ◽  
Author(s):  
Dorothy J. Ball ◽  
Clive A. Slaughter ◽  
Preston Hensley ◽  
William T. Garrard
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Terminal Domain ◽  
Calf Thymus
Sign in / Sign up

Export Citation Format

Share Document