Bacteria sequences

Fur-like proteins are found in nearly all bacteria sequenced so far, with some notable exceptions the highly adapted and specialized pathogens, such as Mycoplasma pneumoniae, M. genitalium, Treponema pallidum, Chlamydia, and Ricketsia do not seem to contain genes encoding Fur-like proteins. Only some of the archaea, e.g. Archaeoglobusfulgidus, encode a Fur-like protein. In many cases, the Fur-like proteins... 

Restriction Endonuclease Bacteria Sequence Recognized" Ends"... 

Eagan, M.J. and Saier, M.H., Jr. (1994) P-type ATPases of eukaryotes and bacteria sequence analyses and construction of phylogenetic trees. J Mol Evol 38, 57-99. 

Human insulin was the first animal protein to be made in bacteria in a sequence identical to the human pancreatic peptide. Expression of separate insulin A and B chains were achieved in Echerichia coli K-12 using genes for the insulin A and B chains synthesized and cloned in frame with the... 

After a desired clone is obtained and mapped with restriction enzymes, further analysis usually depends on the deterrnination of its nucleotide sequence. The nucleotide sequence of a new gene often provides clues to its function and the stmcture of the gene product. Additionally, the DNA sequence of a gene provides a guidepost for further manipulation of the sequence, for example, lea ding to the production of a recombinant protein in bacteria. 

Replication of the Recombinant DNA. In bacteria, repHcation of the recombinant DNA is provided by origin sequences, derived usually... 

The biosynthetic sequence for other aerobic bacteria appears, where known, to be similar to that in Pseudomonas dentrificans although the genes involved, and thus the enzymes, exhibit differences. 

Many proteins that switch off or on gene expression in bacteria are dimeric molecules, and the DNA sequences that they specifically recognize are palindromic at their ends. The twofold symmetry of the protein is therefore matched by twofold symmetry at the ends of the recognition sequence. 

Gram-negative bacteria are surrounded by two membranes, an inner plasma membrane and an outer membrane. These are separated by a periplasmic space. Most plasma membrane proteins contain long, continuous sequences of about 20 hydrophobic residues that are typical of transmembrane a helices such as those found in bacteriorhodopsin. In contrast, most outer membrane proteins do not show such sequence patterns. 

The light-harvesting complex LHl is directly associated with the reaction center in purple bacteria and is therefore referred to as the core or inner antenna, whereas LH2 is known as the peripheral antenna. Both are huilt up from hydrophohic a and p polypeptides of similar size and with low hut significant sequence similarity. The two histidines that hind to chlorophyll with absorption maxima at 850 nm in the periplasmic ring of LH2 are also present in LHl, but the sequence involved in binding the third chlorophyll in LH2 is quite different in LHl. Not surprisingly, the chlorophyll molecules of the periplasmic ring are present in LHl but the chlorophyll molecules with the 800 nm absorption maximum are absent. 

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