scholarly journals A Highly Selective Oligopeptide Binding Protein from the Archaeon Sulfolobus Solfataricus

2010 ◽  
Vol 192 (12) ◽  
pp. 3123-3131 ◽  
Author(s):  
M. Gogliettino ◽  
M. Balestrieri ◽  
G. Pocsfalvi ◽  
I. Fiume ◽  
L. Natale ◽  
...  
Keyword(s):  
Cell Surface ◽  
Binding Protein ◽  
Sulfolobus Solfataricus ◽  
Binding Activity ◽  
Protein Accumulation ◽  
Reading Frame ◽  
Typical Sequence ◽  
Hybrid Complex ◽  
Genes Encoding ◽  
A Cell

ABSTRACT SSO1273 of Sulfolobus solfataricus was identified as a cell surface-bound protein by a proteomics approach. Sequence inspection of the genome revealed that the open reading frame of sso1273 is associated in an operon-like structure with genes encoding all the remaining components of a canonical protein-dependent ATP-binding cassette (ABC) transporter. sso1273 gene expression and SSO1273 protein accumulation on the cell surface were demonstrated to be strongly induced by the addition of a peptide mixture (tryptone) to the culture medium. The native protein was obtained in multimeric form, mostly hexameric, under the purification conditions used, and it was characterized as an oligopeptide binding protein, named S. solfataricus OppA (OppASs). OppaASs possesses typical sequence patterns required for glycosylphosphatidylinositol lipid anchoring, resulting in an N-linked glycoprotein with carbohydrate moieties likely composed of high mannose and/or hybrid complex carbohydrates. OppASs specifically binds oligopeptides and shows a marked selectivity for the amino acid composition of substrates when assayed in complex peptide mixtures. Moreover, a truncated version of OppASs, produced in recombinant form and including the putative binding domain, showed a low but significant oligopeptide binding activity.

scholarly journals Comparison of the Fibronectin-Binding Protein FNE fromStreptococcus equi Subspecies equi with FNZ from S. equi Subspecies zooepidemicus Reveals a Major and Conserved Difference

2001 ◽  
Vol 69 (5) ◽  
pp. 3159-3163 ◽  
Author(s):  
Hans Lindmark ◽  
Martin Nilsson ◽  
Bengt Guss
Keyword(s):  
Dna Sequences ◽  
Stop Codon ◽  
Binding Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Surface Protein ◽  
Binding Activity ◽  
Base Pairs ◽  
Reading Frame ◽  
A Cell

ABSTRACT The gene fnz from Streptococcus equisubspecies zooepidemicus encodes a cell surface protein that binds fibronectin (Fn). Fifty tested isolates of S. equi subspecies equi all contain DNA sequences with similarity to fnz. This work describes the cloning and sequencing of a gene, designated fne, with similarity tofnz from two S. equi subspeciesequi isolates. The DNA sequences were found to be identical in the two strains, and sequence comparison of the fne andfnz genes revealed only minor differences. However, one base deletion was found in the middle of the fne gene and eight base pairs downstream of the altered reading frame there is a stop codon. An Fn-binding protein was purified from the growth medium of a subspecies equi culture. Determination of the NH2-terminal amino acid sequence and molecular mass, as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, revealed that the purified protein is the gene product of the 5′-terminal half of fne. Fn-binding activity has earlier only been found in the COOH-terminal half of FNZ. By the use of a purified recombinant protein containing the NH2 half of FNZ, we provide here evidence that this half of the protein also harbors an Fn-binding domain.

scholarly journals A Novel Cell Surface-Anchored Cellulose-Binding Protein Encoded by the sca Gene Cluster of Ruminococcus flavefaciens

2007 ◽  
Vol 189 (13) ◽  
pp. 4774-4783 ◽  
Author(s):  
Marco T. Rincon ◽  
Tadej Cepeljnik ◽  
Jennifer C. Martin ◽  
Yoav Barak ◽  
Raphael Lamed ◽  
...  
Keyword(s):  
Cell Surface ◽  
Binding Protein ◽  
Scaffolding Proteins ◽  
Ruminococcus Flavefaciens ◽  
Reading Frame ◽  
C Terminus ◽  
A Cell ◽  
Mutant Derivative ◽  
Cellulose Binding ◽  
Recombinant Fragments

ABSTRACT Ruminococcus flavefaciens produces a cellulosomal enzyme complex, based on the structural proteins ScaA, -B, and -C, that was recently shown to attach to the bacterial cell surface via the wall-anchored protein ScaE. ScaA, -B, -C, and -E are all cohesin-bearing proteins encoded by linked genes in the sca cluster. The product of an unknown open reading frame within the sca cluster, herein designated CttA, is similar in sequence at its C terminus to the corresponding region of ScaB, which contains an X module together with a dockerin sequence. The ScaB-XDoc dyad was shown previously to interact tenaciously with the cohesin of ScaE. Likewise, avid binding was confirmed between purified recombinant fragments of the CttA-XDoc dyad and the ScaE cohesin. In addition, the N-terminal regions of CttA were shown to bind to cellulose, thus suggesting that CttA is a cell wall-anchored, cellulose-binding protein. Proteomic analysis showed that the native CttA protein (∼130 kDa) corresponds to one of the three most abundant polypeptides binding tightly to insoluble cellulose in cellulose-grown R. flavefaciens 17 cultures. Interestingly, this protein was also detected among cellulose-bound proteins in the related strain R. flavefaciens 007C but not in a mutant derivative, 007S, that was previously shown to have lost the ability to grow on dewaxed cotton fibers. In R. flavefaciens, the presence of CttA on the cell surface is likely to provide an important mechanism for substrate binding, perhaps compensating for the absence of an identified cellulose-binding module in the major cellulosomal scaffolding proteins of this species.

scholarly journals Human Cytomegalovirus Open Reading Frame TRL11/IRL11 Encodes an Immunoglobulin G Fc-Binding Protein

2001 ◽  
Vol 75 (22) ◽  
pp. 11218-11221 ◽  
Author(s):  
Brendan N. Lilley ◽  
Hidde L. Ploegh ◽  
Rebecca S. Tirabassi
Keyword(s):  
Human Cytomegalovirus ◽  
Immunoglobulin G ◽  
Binding Protein ◽  
Fc Receptors ◽  
Binding Activity ◽  
Open Reading Frame ◽  
Membrane Glycoprotein ◽  
Type I ◽  
Reading Frame

ABSTRACT Several herpesviruses encode Fc receptors that may play a role in preventing antibody-mediated clearance of the virus in vivo. Human cytomegalovirus (HCMV) induces an Fc-binding activity in cells upon infection, but the gene that encodes this Fc-binding protein has not been identified. Here, we demonstrate that the HCMV AD169 open reading frame TRL11 and its identical copy, IRL11, encode a type I membrane glycoprotein that possesses IgG Fc-binding capabilities.

Biochemical Characterization of the Histidine Triad Protein PhtD as a Cell Surface Zinc-Binding Protein of Pneumococcus

Biochemistry ◽  
2011 ◽  
Vol 50 (17) ◽  
pp. 3551-3558 ◽  
Author(s):  
Elodie Loisel ◽  
Suneeta Chimalapati ◽  
Catherine Bougault ◽  
Anne Imberty ◽  
Benoit Gallet ◽  
...  
Keyword(s):  
Cell Surface ◽  
Biochemical Characterization ◽  
Binding Protein ◽  
Zinc Binding ◽  
A Cell

scholarly journals Cysteine Biosynthesis Pathway in the ArchaeonMethanosarcina barkeri Encoded by Acquired Bacterial Genes?

2000 ◽  
Vol 182 (1) ◽  
pp. 143-145 ◽  
Author(s):  
Makoto Kitabatake ◽  
Man Wah So ◽  
Debra L. Tumbula ◽  
Dieter Söll
Keyword(s):  
Sulfolobus Solfataricus ◽  
Methanosarcina Barkeri ◽  
Archaeoglobus Fulgidus ◽  
Biosynthesis Pathway ◽  
Cysteine Biosynthesis ◽  
Gene Encoding ◽  
Reading Frame ◽  
Genome Data ◽  
Genes Encoding ◽  
Bacterial Genes

ABSTRACT The pathway of cysteine biosynthesis in archaea is still unexplored. Complementation of a cysteine auxotrophic Escherichia coli strain NK3 led to the isolation of the Methanosarcina barkeri cysK gene [encoding O-acetylserine (thiol)-lyase-A], which displays great similarity to bacterialcysK genes. Adjacent to cysK is an open reading frame orthologous to bacterial cysE (serine transacetylase) genes. These two genes could account for cysteine biosynthesis in this archaeon. Analysis of recent genome data revealed the presence of bacteria-like cysM genes [encodingO-acetylserine (thiol)-lyase-B] in Pyrococcusspp., Sulfolobus solfataricus, and Thermoplasma acidophilum. However, no orthologs for these genes can be found in Methanococcus jannaschii, Methanobacterium thermoautotrophicum, and Archaeoglobus fulgidus, implying the existence of unrecognizable genes for the same function or a different cysteine biosynthesis pathway.

scholarly journals Photoaffinity Labeling of a Cell Surface Polyamine Binding Protein

1995 ◽  
Vol 270 (48) ◽  
pp. 28705-28711 ◽  
Author(s):  
Donna M. Felschow ◽  
Joan MacDiarmid ◽  
Thomas Bardos ◽  
Ronghui Wu ◽  
Patrick M. Woster ◽  
...  
Keyword(s):  
Cell Surface ◽  
Binding Protein ◽  
Photoaffinity Labeling ◽  
A Cell

The ovine pancreatic protein which binds insulin-like growth factor binding protein-3 is procarboxypeptidase A

1996 ◽  
Vol 150 (1) ◽  
pp. 51-56 ◽  
Author(s):  
P J Fowke ◽  
S C Hodgkinson
Keyword(s):  
Growth Factor ◽  
Cell Surface ◽  
Binding Protein ◽  
Binding Activity ◽  
Insulin Like Growth Factor ◽  
Surface Binding ◽  
Factor Binding ◽  
Amino Terminal ◽  
Igf I ◽  
Igfbp 3

Abstract Insulin-like growth factor binding protein-3 (IGFBP-3) is known to modulate the actions of insulin-like growth factors (IGF)-I and -II at the level of the cell. Proposed mechanisms include association of IGFBP-3 with cell surface proteoglycan, with cell surface binding proteins, proteolysis and/or internalization of IGFBP-3. In previous studies we have characterized a protein of 40 kDa in extracts of ovine pancreas and muscle which binds IGFBP-3 on ligand blot analyses. This paper reports the identity of the pancreatic species as procarboxypeptidase A (peptidyl-l-amino acid hydrolase, E.C. 3.4.17.1; proCPA). Identity was established by amino terminal sequence analysis, binding studies with pure bovine carboxypeptidase A (CPA) and observations that the binding activity was present in pancreatic secretions consistent with the role of proCPA as a secretory zymogen. The binding activity was inhibited by unlabelled IGFBP-3 at high doses (10 μg/ml) and reduced but not abolished by preincubation of 125I-IGFBP-3 with excess IGF-I. Digestion of 125I-IGFBP-3 with mature CPA produced a 26 kDa product. Modification of IGFBP-3 by CPA or binding to proCPA may provide a mechanism for modulation of IGFBP activity and hence IGF action. Journal of Endocrinology (1996) 150, 51–56

The titanium binding protein ofRhodococcus ruberGIN1 (NCIMB 40340) is a cell-surface homolog of the cytosolic enzyme dihydrolipoamide dehydrogenase

2009 ◽  
Vol 22 (2) ◽  
pp. 138-145 ◽  
Author(s):  
Ari Siegmann ◽  
Avital Komarska ◽  
Yifaat Betzalel ◽  
Irene Brudo ◽  
Sadanari Jindou ◽  
...  
Keyword(s):  
Cell Surface ◽  
Binding Protein ◽  
Dihydrolipoamide Dehydrogenase ◽  
A Cell
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