The Comparative Analysis of Two Homologous Genomic Islands Associated with the Noncoding Sequence in Enterobacter cloacae

2013 ◽  
Vol 448-453 ◽  
pp. 3-6
Author(s):  
Jiao Zhang ◽  
Lei Song
Keyword(s):  
Structural Characteristics ◽  
Enterobacter Cloacae ◽  
Protein Assembly ◽  
Genomic Islands ◽  
Noncoding Sequence ◽  
Flanking Sequence ◽  
Hypothetical Gene ◽  
Evolution Pattern ◽  
Bacteriophage P2 ◽  
Coat Protein Assembly

The genomic islands (GIs) are usually the products of horizontal gene transfer (HGT) that is evolution pattern in prokaryote. Two homologous GIs (WSU1GINoand KU01GINo) containing the homologous integrase of Bacteriophage P2 were determined inEnterobacter cloacaethrough flanking sequence alignment of the homologous integrase. The homologous GIs were integrated into the noncoding sequence. Their common flanking sequence is 5-AAGGCTCCCTCAGGAGC-3, and their integrases share 97% similarity. About two-thirds of the nucleotide sequences between WSU1GINoand KU01GINoare highly similar. The different regions between WSU1GINoand KU01GINomainly include hypothetical gene, Phage-related tail gene, capsid gene, and baseplate assembly gene. In conclusion, the tandem arrangement of WSU1GINoand KU01GINowill be artificially constructed because of their similar structural characteristics, and phage coat protein assembly will also be analyzed.

Analysis of RNA phage fr coat protein assembly by insertion, deletion and substitution mutagenesis

1993 ◽  
Vol 6 (8) ◽  
pp. 883-891 ◽  
Author(s):  
P. Pushko ◽  
T. Kozlovskaya ◽  
I. Sominskaya ◽  
A. Brede ◽  
E. Stankevica ◽  
...  
Keyword(s):  
Coat Protein ◽  
Protein Assembly ◽  
Coat Protein Assembly ◽  
Rna Phage

Structural characteristics of genomic islands associated withRlmHgenes inBacillus

2017 ◽  
pp. 263-268
Author(s):  
Lingwei Su ◽  
Xuan Peng ◽  
Qingze Zha ◽  
Shidan He ◽  
Mengjie Yang ◽  
...  
Keyword(s):  
Structural Characteristics ◽  
Genomic Islands

The Structural Characteristics and Function Analysis of the Mobile Genomic Islands Flanked by Isocitrate Dehydrogenase Genes in Escherichia coli and Salmonella enterica

2012 ◽  
Vol 482-484 ◽  
pp. 2218-2222
Author(s):  
Lei Song ◽  
Xue Hong Zhang
Keyword(s):  
Escherichia Coli ◽  
Isocitrate Dehydrogenase ◽  
Salmonella Enterica ◽  
Function Analysis ◽  
Structural Characteristics ◽  
Genomic Islands ◽  
Transposase Gene ◽  
Integrase Gene ◽  
Mobile Gene ◽  
And Function

Eleven genomic islands (GIs) flanked by isocitrate dehydrogenase genes are determined in Escherichia coli and Salmonella enterica. These GIs have at least one mobile gene, such as integrase gene, transposase gene or recombinase gene. Through annotation of internal genes, these GIs are related to lambda prophage. The excisionase gene is associated with the mobile gene in some GIs. An ABC transporter, namely, sitABCD operon, is existed in some GIs and may uptake Fe2+ and Mn2+. Mn2+ is a second cofactor and an essential activator of the isocitrate dehydrogenase. The cleavage site of functional lambda integrase is 5’-TGCTGCGCCA-3’ in direct repeats at 3’-end of icd gene.The truncated lambda integrases (ECP_1132 and ECP_1135) are inactive because the transposon inserted the integrase gene by 5’-CCTGG-3’. This Fe2+/Mn2+ transport operon is predicted that is a recent product of horizontal gene transfer in E. coli because this operon is also existed in S. enterica and is not in a mobile GIs.

scholarly journals Functional Regions of the Bacillus subtilis Spore Coat Morphogenetic Protein CotE

1999 ◽  
Vol 181 (22) ◽  
pp. 7043-7051 ◽  
Author(s):  
Tamara Bauer ◽  
Shawn Little ◽  
Axel G. Stöver ◽  
Adam Driks
Keyword(s):  
Amino Acids ◽  
Bacillus Subtilis ◽  
Amino Acid ◽  
Coat Protein ◽  
Protein Assembly ◽  
Spore Coat ◽  
Coat Proteins ◽  
Outer Coat ◽  
Bacillus Subtilis Spore ◽  
Coat Protein Assembly

ABSTRACT The Bacillus subtilis spore is encased in a resilient, multilayered proteinaceous shell, called the coat, that protects it from the environment. A 181-amino-acid coat protein called CotE assembles into the coat early in spore formation and plays a morphogenetic role in the assembly of the coat’s outer layer. We have used a series of mutant alleles of cotE to identify regions involved in outer coat protein assembly. We found that the insertion of a 10-amino-acid epitope, between amino acids 178 and 179 of CotE, reduced or prevented the assembly of several spore coat proteins, including, most likely, CotG and CotB. The removal of 9 or 23 of the C-terminal-most amino acids resulted in an unusually thin outer coat from which a larger set of spore proteins was missing. In contrast, the removal of 37 amino acids from the C terminus, as well as other alterations between amino acids 4 and 160, resulted in the absence of a detectable outer coat but did not prevent localization of CotE to the forespore. These results indicate that changes in the C-terminal 23 amino acids of CotE and in the remainder of the protein have different consequences for outer coat protein assembly.

A High Resolution Study of G.P. Zones in Aluminum - 4.2 at % Silver

1982 ◽  
Vol 40 ◽  
pp. 722-723 ◽  
Author(s):  
R. Gronsky
Keyword(s):  
Electron Microscopy ◽  
Transmission Electron Microscopy ◽  
High Resolution ◽  
Computer Simulations ◽  
Structural Characteristics ◽  
X Ray Diffraction ◽  
X Ray ◽  
Transmission Electron ◽  
Resolution Study

The phenomenon of clustering in Al-Ag alloys has been extensively studied since the early work of Guinierl, wherein the pre-precipitation state was characterized as an assembly of spherical, ordered, silver-rich G.P. zones. Subsequent x-ray and TEM investigations yielded results in general agreement with this model. However, serious discrepancies were later revealed by the detailed x-ray diffraction - based computer simulations of Gragg and Cohen, i.e., the silver-rich clusters were instead octahedral in shape and fully disordered, atleast below 170°C. The object of the present investigation is to examine directly the structural characteristics of G.P. zones in Al-Ag by high resolution transmission electron microscopy.

SEM analysis of the change in the reaction rates with deposit structures in the copper-iron cementation system

1978 ◽  
Vol 36 (1) ◽  
pp. 456-457
Author(s):  
V. Annamalai ◽  
L.E. Murr
Keyword(s):  
Structural Characteristics ◽  
Secondary Electron Emission ◽  
Copper Deposit ◽  
Reaction Rates ◽  
Sem Analysis ◽  
Experimental Conditions ◽  
Major Drawback ◽  
Emission Mode ◽  
Scrap Iron ◽  
Image Position

Economical recovery of copper metal from leach liquors has been carried out by the simple process of cementing copper onto a suitable substrate metal, such as scrap-iron, since the 16th century. The process has, however, a major drawback of consuming more iron than stoichiometrically needed by the reaction.Therefore, many research groups started looking into the process more closely. Though it is accepted that the structural characteristics of the resultant copper deposit cause changes in reaction rates for various experimental conditions, not many systems have been systematically investigated. This paper examines the deposit structures and the kinetic data, and explains the correlations between them.A simple cementation cell along with rotating discs of pure iron (99.9%) were employed in this study to obtain the kinetic results The resultant copper deposits were studied in a Hitachi Perkin-Elmer HHS-2R scanning electron microscope operated at 25kV in the secondary electron emission mode.

Use of 2½ D imaging in analysis of NiTi martensite

1978 ◽  
Vol 36 (1) ◽  
pp. 610-611
Author(s):  
G. M. Michal
Keyword(s):  
Memory Effect ◽  
Monoclinic Phase ◽  
Reaction Path ◽  
Structural Characteristics ◽  
Salient Feature ◽  
Martensite Phase ◽  
Orientation Relationships ◽  
Low Symmetry ◽  
Hydride Phases ◽  
Unusual Shape

Several TEM investigations have attempted to correlate the structural characteristics to the unusual shape memory effect in NiTi, the consensus being the essence of the memory effect is ostensible manifest in the structure of NiTi transforming martensitic- ally from a B2 ordered lattice to a low temperature monoclinic phase. Commensurate with the low symmetry of the martensite phase, many variants may form from the B2 lattice explaining the very complex transformed microstructure. The microstructure may also be complicated by the enhanced formation of oxide or hydride phases and precipitation of intermetallic compounds by electron beam exposure. Variants are typically found in selfaccommodation groups with members of a group internally twinned and the twins themselves are often observed to be internally twinned. Often the most salient feature of a group of variants is their close clustering around a given orientation. Analysis of such orientation relationships may be a key to determining the nature of the reaction path that gives the transformation its apparently perfect reversibility.

Use of light microscopy in the qualitative and quantitative study of liquid crystalline order

1992 ◽  
Vol 50 (1) ◽  
pp. 264-265
Author(s):  
Christopher Viney
Keyword(s):  
Light Microscopy ◽  
Liquid Crystalline ◽  
Structural Characteristics ◽  
Molecular Order ◽  
Liquid Crystalline Phases ◽  
Convenient Technique ◽  
Liquid Crystalline Materials ◽  
Transparent Windows

Light microscopy is a convenient technique for characterizing molecular order in fluid liquid crystalline materials. Microstructures can usually be observed under the actual conditions that promote the formation of liquid crystalline phases, whether or not a solvent is required, and at temperatures that can range from the boiling point of nitrogen to 600°C. It is relatively easy to produce specimens that are sufficiently thin and flat, simply by confining a droplet between glass cover slides. Specimens do not need to be conducting, and they do not have to be maintained in a vacuum. Drybox or other controlled environmental conditions can be maintained in a sealed chamber equipped with transparent windows; some heating/ freezing stages can be used for this purpose. It is relatively easy to construct a modified stage so that the generation and relaxation of global molecular order can be observed while specimens are being sheared, simulating flow conditions that exist during processing. Also, light only rarely affects the chemical composition or molecular weight distribution of the sample. Because little or no processing is required after collecting the sample, one can be confident that biologically derived materials will reveal many of their in vivo structural characteristics, even though microscopy is performed in vitro.

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