scholarly journals Structure of the N-terminal fragment ofEscherichia coliLon protease

2010 ◽  
Vol 66 (8) ◽  
pp. 865-873 ◽  
Author(s):  
Mi Li ◽  
Alla Gustchina ◽  
Fatima S. Rasulova ◽  
Edward E. Melnikov ◽  
Michael R. Maurizi ◽  
...  
Keyword(s):  
Binding Sites ◽  
Spatial Relationship ◽  
Anomalous Scattering ◽  
Lon Protease ◽  
Binding Domains ◽  
Acid Protein ◽  
Α Helix ◽  
Almost All ◽  
Relationship Of ◽  
Amino Acid Protein

The structure of a recombinant construct consisting of residues 1–245 ofEscherichia coliLon protease, the prototypical member of the A-type Lon family, is reported. This construct encompasses all or most of the N-terminal domain of the enzyme. The structure was solved by SeMet SAD to 2.6 Å resolution utilizing trigonal crystals that contained one molecule in the asymmetric unit. The molecule consists of two compact subdomains and a very long C-terminal α-helix. The structure of the first subdomain (residues 1–117), which consists mostly of β-strands, is similar to that of the shorter fragment previously expressed and crystallized, whereas the second subdomain is almost entirely helical. The fold and spatial relationship of the two subdomains, with the exception of the C-terminal helix, closely resemble the structure of BPP1347, a 203-amino-acid protein of unknown function fromBordetella parapertussis, and more distantly several other proteins. It was not possible to refine the structure to satisfactory convergence; however, since almost all of the Se atoms could be located on the basis of their anomalous scattering the correctness of the overall structure is not in question. The structure reported here was also compared with the structures of the putative substrate-binding domains of several proteins, showing topological similarities that should help in defining the binding sites used by Lon substrates.

glsA, a Volvox gene required for asymmetric division and germ cell specification, encodes a chaperone-like protein

Development ◽  
1999 ◽  
Vol 126 (4) ◽  
pp. 649-658 ◽  
Author(s):  
S.M. Miller ◽  
D.L. Kirk
Keyword(s):  
Mitotic Spindle ◽  
Site Directed Mutagenesis ◽  
Cell Specification ◽  
Division Plane ◽  
Binding Domains ◽  
Acid Protein ◽  
Germ Cell Specification ◽  
Asymmetric Divisions ◽  
Dividing Cells ◽  
Amino Acid Protein

The gls genes of Volvox are required for the asymmetric divisions that set apart cells of the germ and somatic lineages during embryogenesis. Here we used transposon tagging to clone glsA, and then showed that it is expressed maximally in asymmetrically dividing embryos, and that it encodes a 748-amino acid protein with two potential protein-binding domains. Site-directed mutagenesis of one of these, the J domain (by which Hsp40-class chaperones bind to and activate specific Hsp70 partners) abolishes the capacity of glsA to rescue mutants. Based on this and other considerations, including the fact that the GlsA protein is associated with the mitotic spindle, we discuss how it might function, in conjunction with an Hsp70-type partner, to shift the division plane in asymmetrically dividing cells.

scholarly journals DNA-binding activities of the Drosophila melanogaster even-skipped protein are mediated by its homeo domain and influenced by protein context.

1988 ◽  
Vol 8 (11) ◽  
pp. 4598-4607 ◽  
Author(s):  
T Hoey ◽  
R Warrior ◽  
J Manak ◽  
M Levine
Keyword(s):  
Dna Binding ◽  
Binding Sites ◽  
Consensus Sequence ◽  
Binding Properties ◽  
Binding Behavior ◽  
High Affinity ◽  
Homeo Box ◽  
Acid Protein ◽  
Dna Binding Properties ◽  
Amino Acid Protein

The homeo box gene even-skipped (eve) encodes a 376-amino-acid protein that binds with high affinity to sequences located near the 5' termini of the eve and en genes. The 5' en sites are A + T rich and contain copies of the 10-base-pair (bp) consensus sequence T-C-A-A-T-T-A-A-A-T. In contrast, the 5' eve sites are G + C rich and contain the 9-bp sequence T-C-A-G-C-A-C-C-G. Among the five different homeo box proteins that have been tested for binding, eve is unique in that it shows virtually equal preference for the A + T-rich 5' en binding sites and the G + C-rich 5' eve sites. Most of the other proteins bind with a relatively higher affinity to the en sites than to the eve sites. In an effort to identify the regions of the eve protein that are responsible for its efficient binding to both classes of recognition sequences, we analyzed the DNA-binding properties of various mutant eve proteins. These studies suggest that the homeo domain of the eve protein is responsible for both binding activities. However, mutations in distant regions of the protein influenced the binding behavior of the eve homeo domain and caused a reduction in binding to the G + C class of recognition sites. We propose that the protein context of the homeo domain can influence its DNA-binding properties.

Spatial relationship of the Fis binding sites for Hin recombinational enhancer activity

Nature ◽  
1987 ◽  
Vol 329 (6138) ◽  
pp. 462-465 ◽  
Author(s):  
Reid C. Johnson ◽  
Anna C. Glasgow ◽  
Melvin I. Simon
Keyword(s):  
Binding Sites ◽  
Spatial Relationship ◽  
Enhancer Activity ◽  
Relationship Of

Terbium(III) luminescence study of the spatial relationship of tryptophan residues to the two metal ion binding sites of Escherichia coli glutamine synthetase

Biochemistry ◽  
1991 ◽  
Vol 30 (14) ◽  
pp. 3417-3421 ◽  
Author(s):  
Linda S. McNemar ◽  
Wann Yin Lin ◽  
Charles D. Eads ◽  
William M. Atkins ◽  
Patrice Dombrosky ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Sites ◽  
Metal Ion ◽  
Spatial Relationship ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Tryptophan Residues ◽  
Ion Binding Sites ◽  
Relationship Of ◽  
Metal Ion Binding Sites

DNA-binding activities of the Drosophila melanogaster even-skipped protein are mediated by its homeo domain and influenced by protein context

1988 ◽  
Vol 8 (11) ◽  
pp. 4598-4607
Author(s):  
T Hoey ◽  
R Warrior ◽  
J Manak ◽  
M Levine
Keyword(s):  
Dna Binding ◽  
Binding Sites ◽  
Consensus Sequence ◽  
Binding Properties ◽  
Binding Behavior ◽  
High Affinity ◽  
Homeo Box ◽  
Acid Protein ◽  
Dna Binding Properties ◽  
Amino Acid Protein

The homeo box gene even-skipped (eve) encodes a 376-amino-acid protein that binds with high affinity to sequences located near the 5' termini of the eve and en genes. The 5' en sites are A + T rich and contain copies of the 10-base-pair (bp) consensus sequence T-C-A-A-T-T-A-A-A-T. In contrast, the 5' eve sites are G + C rich and contain the 9-bp sequence T-C-A-G-C-A-C-C-G. Among the five different homeo box proteins that have been tested for binding, eve is unique in that it shows virtually equal preference for the A + T-rich 5' en binding sites and the G + C-rich 5' eve sites. Most of the other proteins bind with a relatively higher affinity to the en sites than to the eve sites. In an effort to identify the regions of the eve protein that are responsible for its efficient binding to both classes of recognition sequences, we analyzed the DNA-binding properties of various mutant eve proteins. These studies suggest that the homeo domain of the eve protein is responsible for both binding activities. However, mutations in distant regions of the protein influenced the binding behavior of the eve homeo domain and caused a reduction in binding to the G + C class of recognition sites. We propose that the protein context of the homeo domain can influence its DNA-binding properties.

scholarly journals An Archaeal Aerotaxis Transducer Combines Subunit I Core Structures of Eukaryotic Cytochrome c Oxidase and Eubacterial Methyl-Accepting Chemotaxis Proteins

1998 ◽  
Vol 180 (7) ◽  
pp. 1642-1646 ◽  
Author(s):  
Alexei Brooun ◽  
James Bell ◽  
Tracey Freitas ◽  
Randy W. Larsen ◽  
Maqsudul Alam
Keyword(s):  
Binding Sites ◽  
Gene Sequence ◽  
Halobacterium Salinarum ◽  
Heme Binding ◽  
Transmembrane Segments ◽  
Acid Protein ◽  
N Terminus ◽  
Chemotaxis Proteins ◽  
Functional Features ◽  
Amino Acid Protein

ABSTRACT Signal transduction in the archaeon Halobacterium salinarum is mediated by three distinct subfamilies of transducer proteins. Here we report the complete htrVIII gene sequence and present analysis of the encoded primary structure and its functional features. HtrVIII is a 642-amino-acid protein and belongs to halobacterial transducer subfamily B. At the N terminus, the protein contains six transmembrane segments that exhibit homology to the heme-binding sites of the eukaryotic cytochrome c oxidase. The C-terminal domain has high homology with the eubacterial methyl-accepting chemotaxis protein. The HtrVIII protein mediates aerotaxis: a strain with a deletion of the htrVIII gene loses aerotaxis, while an overproducing strain exhibits stronger aerotaxis. We also demonstrate that HtrVIII is a methyl-accepting protein and demethylates during the aerotaxis response.

Pharmaceutical Standardization of Saptamrita Lauha

2016 ◽  
Vol 1 (3) ◽  
Author(s):  
Dr. Pranav K. Shah ◽  
L B. Singh ◽  
P U Vaishnav ◽  
Bharat Kalsariya
Keyword(s):  
Large Scale ◽  
Oral Route ◽  
Water Soluble ◽  
Scale Production ◽  
External Application ◽  
Chemical Screening ◽  
Large Scale Production ◽  
Acid Protein ◽  
Almost All ◽  
Amino Acid Protein

Shalakya Tantra is a one of the branch of Ashtanga Ayurveda and Netra Chikitsa is a part of Shalakya Tantra. There are so many formulations are mentioned in the treatment of Netra Roga by oral route as well as external application, Saptamrita Lauha is one of them. It is a very popular, very safe and effective formulation for eye diseases. In Ayurveda classics there are so many references are available for Saptamrita Lauha. These formulation are mainly described in Netra Roga and Shoola Roga in almost all the books. In majority references Saptamrita Lauha powder is taken with Anupana or Sahapana of honey and ghee. Sundar Ayurveda Teaching Pharmacy is also manufacturing many batches of Saptamrita Lauha with the reference from Bheshaja Samhita, chapter 4/54, Loha andMandura Kalpana and follow the in house quality control parameters to standardized the medicine in large scale production. The particle size of Saptamrita Lauha is 3.2 μm to 3.8 μm, pH from 6.0 to 6.9,loss on drying from 1.2 % to 1.8%, ash value 16.2 %w/w to 24.5 %w/w, acid insoluble ash value from 2.6 %w/w to3.6 %w/w, alcohol soluble extractive value from 42.9% v/w to 47.7 %v/w, water soluble extractive value from 21.1 % to 26.8%. Phyto-chemical screening of Saptamrita Lauha shows Glycoside, Amino acid, Protein, Carbohydrate, Flavanoid, Tannin, Steroid, Saponin and Alkaloid were present in all batches. On the basis of this study it’s clear that, if we follow the same procedure with authentic drugs then large scale production also having Quality assurance.

Ultrastructural evidence for mast cell-macrophage interrelationships in the dura mater of the rat: Infrequent mast cell-nerve associations

1990 ◽  
Vol 48 (3) ◽  
pp. 352-353
Author(s):  
Ruth V.W. Dimlich
Keyword(s):  
Mast Cell ◽  
Mast Cells ◽  
Dura Mater ◽  
Spatial Relationship ◽  
Potassium Phosphate ◽  
Plasma Extravasation ◽  
Close Spatial Relationship ◽  
Male Wistar Rats ◽  
Headache Pain ◽  
Relationship Of

Mast cells in the dura mater of the rat may play a role in cerebral pathologies including neurogenic inflammation (vasodilation; plasma extravasation) and headache pain . As has been suggested for other tissues, dural mast cells may exhibit a close spatial relationship to nerves. There has been no detailed ultrastructural description of mast cells in this tissue; therefore, the goals of this study were to provide this analysis and to determine the spatial relationship of mast cells to nerves and other components of the dura mater in the rat.Four adult anesthetized male Wistar rats (290-400 g) were fixed by perfusion through the heart with 2% glutaraldehyde and 2.8% paraformaldehyde in a potassium phosphate buffer (pH 7.4) for 30 min. The head of each rat was removed and stored in fixative for a minimum of 24 h at which time the dural coverings were removed and dissected into samples that included the middle meningeal vasculature. Samples were routinely processed and flat embedded in LX 112. Thick (1 um) sections from a minimum of 3 blocks per rat were stained with toluidine blue (0.5% aqueous).

scholarly journals Crayfish hemocytes develop along the granular cell lineage

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Fang Li ◽  
Zaichao Zheng ◽  
Hongyu Li ◽  
Rongrong Fu ◽  
Limei Xu ◽  
...  
Keyword(s):  
Developmental Stages ◽  
Cell Lineage ◽  
Granular Cell ◽  
Marker Genes ◽  
Hematopoietic Tissue ◽  
Differentiated Cells ◽  
Stage Of Development ◽  
Almost All ◽  
Relationship Of

AbstractDespite the central role of hemocytes in crustacean immunity, the process of hemocyte differentiation and maturation remains unclear. In some decapods, it has been proposed that the two main types of hemocytes, granular cells (GCs) and semigranular cells (SGCs), differentiate along separate lineages. However, our current findings challenge this model. By tracking newly produced hemocytes and transplanted cells, we demonstrate that almost all the circulating hemocytes of crayfish belong to the GC lineage. SGCs and GCs may represent hemocytes of different developmental stages rather than two types of fully differentiated cells. Hemocyte precursors produced by progenitor cells differentiate in the hematopoietic tissue (HPT) for 3 ~ 4 days. Immature hemocytes are released from HPT in the form of SGCs and take 1 ~ 3 months to mature in the circulation. GCs represent the terminal stage of development. They can survive for as long as 2 months. The changes in the expression pattern of marker genes during GC differentiation support our conclusions. Further analysis of hemocyte phagocytosis indicates the existence of functionally different subpopulations. These findings may reshape our understanding of crustacean hematopoiesis and may lead to reconsideration of the roles and relationship of circulating hemocytes.

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