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 apical localization of SGLT1 glucose transporter is determined by the short amino acid sequence in its N-terminal domain

2001 ◽  
Vol 80 (12) ◽  
pp. 765-774 ◽  
Author(s):  
Takeshi Suzuki ◽  
Keiko Fujikura ◽  
Haruko Koyama ◽  
Toshiyuki Matsuzaki ◽  
Yukiko Takahashi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Glucose Transporter ◽  
Terminal Domain ◽  
Short Amino Acid Sequence ◽  
Apical Localization

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 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

scholarly journals Isolation and characterization of different C-terminal fragments of dystrophin expressed in Escherichia coli

1992 ◽  
Vol 288 (3) ◽  
pp. 1037-1044 ◽  
Author(s):  
R E Milner ◽  
J Busaan ◽  
M Michalak
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Fusion Proteins ◽  
Cytoskeletal Proteins ◽  
Terminal Region ◽  
Soluble Form ◽  
E Coli ◽  
Terminal Domain ◽  
Isolation And Characterization

Dystrophin, the protein product of the Duchenne muscular dystrophy gene, is thought to belong to a family of membrane cytoskeletal proteins. Based on its deduced amino-acid sequence, it is postulated to have several distinct structural domains; an N-terminal region; a central, rod-shaped, domain; and a C-terminal domain [Koenig, Monaco & Kunkel (1988) Cell 53, 219-228]. The C-terminal domain is further divided into two regions; the first has some sequence similarity to slime mould alpha-actinin, and is rich in cysteine residues; this is followed by the C-terminal amino-acid sequence that is unique to dystrophin. Dystrophin is very difficult to purify in quantities sufficient for detailed studies of the structure/function relationships within the molecule. Therefore, in this study, we have expressed selected fragments of the C-terminal region of dystrophin, as fusion proteins, in Escherichia coli. Importantly, we describe the first successful purification, from E. coli lysates, of large quantities of fragments of dystrophin in a soluble form. The first fragment, termed CT-1, encodes the C-terminal 201 amino acids of the protein; the second, termed CT-2, spans the cysteine-rich region of the C-terminal domain. These fusion proteins were identified by their mobility in SDS/PAGE, by their interaction with appropriate affinity columns and by their reactivity with anti-dystrophin antibodies. The fragment CT-2, which spans a region containing putative EF-hand-like sequences, was found to bind Ca2+ in 45Ca2+ overlay experiments. In addition, we have discovered that the fragment CT-1, but not fragment CT-2, interacts specifically with the E. coli DnaK gene product [analogue of heat shock protein 70 (hsp70)]. This interaction is disrupted, in vitro, by the addition of ATP. Our results indicate that the two C-terminal fragments of dystrophin have differing biophysical properties, indicating that they may play distinct roles in the function of the protein.

scholarly journals A double leucine within the GLUT4 glucose transporter COOH-terminal domain functions as an endocytosis signal.

1994 ◽  
Vol 126 (4) ◽  
pp. 979-989 ◽  
Author(s):  
S Corvera ◽  
A Chawla ◽  
R Chakrabarti ◽  
M Joly ◽  
J Buxton ◽  
...  
Keyword(s):  
Cell Surface ◽  
Glucose Transporter ◽  
Surface Display ◽  
Cell Surface Display ◽  
Underlying Mechanism ◽  
Terminal Domain ◽  
Amino Acid Region ◽  
Intracellular Compartments ◽  
A Cell ◽  
Glucose Transporter Glut4

The unique COOH-terminal 30-amino acid region of the adipocyte/skeletal muscle glucose transporter (GLUT4) appears to be a major structural determinant of this protein's perinuclear localization, from where it is redistributed to the cell surface in response to insulin. To test whether an underlying mechanism of this domain's function involves glucose transporter endocytosis rates, transfected cells were generated expressing exofacial hemagglutinin epitope (HA)-tagged erythrocyte/brain glucose transporter (GLUT1) or a chimera containing the COOH-terminal 30 amino acids of GLUT4 substituted onto this GLUT1 construct. Incubation of COS-7 or CHO cells expressing the HA-tagged chimera with anti-HA antibody at 37 degrees resulted in an increased rate of antibody internalization compared to cells expressing similar levels of HA-tagged GLUT1, which displays a cell surface disposition. Colocalization of the internalized anti-HA antibody in vesicular structures with internalized transferrin and with total transporters was established by digital imaging microscopy, suggesting the total cellular pool of transporters are continuously recycling through the coated pit endocytosis pathway. Mutation of the unique double leucines 489 and 490 in the rat GLUT4 COOH-terminal domain to alanines caused the HA-tagged chimera to revert to the slow endocytosis rate and steady-state cell surface display characteristic of GLUT1. These results support the hypothesis that the double leucine motif in the GLUT4 COOH terminus operates as a rapid endocytosis and retention signal in the GLUT4 transporter, causing its localization to intracellular compartments in the absence of insulin.

Analysis of Glyceraldehyde 3-Phosphate Dehydrogenase Gene in Lactarius Deliciosus Base on Bioinformatics

2012 ◽  
Vol 429 ◽  
pp. 249-252
Author(s):  
He Li ◽  
Guo Ying Zhou ◽  
Liang Guo ◽  
Ju Nang Liu
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Lactarius Deliciosus ◽  
Terminal Domain ◽  
Glycosylation Sites ◽  
Dehydrogenase Gene ◽  
Carbon Molecules

Glyceraldehyde 3-phosphate dehydrogenase is an enzyme that catalyzes the sixth step of glycolysis and thus serves to break down glucose for energy and carbon molecules. In the present study, some characters of the amino acid sequence of GAPDH of L.deliciosus were predicted and analyzed with the tools of bioinformatics. These results showed that the protein was composed of 20 kinds of amino acid; the theoretical pI of GAPDH was 7.08 and the theoretical molecular weight of GAPDH was 26165.9 Da; the total number of atoms was 3714. It was a stable protein. There were 7 glycosylation sites and it was a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD (P) binding fold. C-terminal domain is a mixed alpha/antiparallel beta fold.

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