CODON DISTRIBUTIONS IN DNA SEQUENCE OF ESCHERICHIA COLI

2002 ◽  
Vol 10 (01) ◽  
pp. 47-60 ◽  
Author(s):  
SU-LONG NYEO ◽  
I-CHING YANG

The distributions of codons in the DNA sequence of Escherichia coli K-12 are studied by using several statistical methods of analysis. Codons corresponding to the amino acids leucine, alanine and isoleucine are considered. The pair distributions of the codons as a function of the pair separation are evaluated and are seen to decay exponentially. The exponential decay constants have a linear relation with the numbers of the codons, indicating that the codons are randomly distributed in the sequence. The pair correlation and power spectral methods also show similar statistical behavior of codons in the sequence, with the exception that there appear very small peaks about the frequency f=0.286 in the power spectra of the amino acids leucine, alanine and isoleucine. Such a frequency reflects a periodicity of about 3.5 amino acids and a general helical structure of the proteins of the bacterium.

1989 ◽  
Vol 171 (9) ◽  
pp. 5169-5172 ◽  
Author(s):  
H Suzuki ◽  
H Kumagai ◽  
T Echigo ◽  
T Tochikura
Keyword(s):  

1989 ◽  
Vol 9 (7) ◽  
pp. 3000-3008
Author(s):  
E A Craig ◽  
J Kramer ◽  
J Shilling ◽  
M Werner-Washburne ◽  
S Holmes ◽  
...  

SSC1 is an essential member of the yeast HSP70 multigene family (E. Craig, J. Kramer, and J. Kosic-Smithers, Proc. Natl. Acad. Sci. USA 84:4156-4160, 1987). Analysis of the SSC1 DNA sequence revealed that it could encode a 70,627-dalton protein that is more similar to DnaK, an Escherichia coli hsp70 protein, than other yeast hsp70s whose sequences have been determined. Ssc1p was found to have an amino-terminal extension of 28 amino acids, in comparison with either Ssa1p, another hsp70 yeast protein, or Dnak. This putative leader is rich in basic and hydroxyl amino acids, characteristic of many mitochondrial leader sequences. Ssc1p that was synthesized in vitro could be imported into mitochondria and was cleaved in the process. The imported protein comigrated with an abundant mitochondrial protein that reacted with hsp70-specific antibodies. We conclude that Ssc1p is a mitochondrial protein and that hsp70 proteins perform functions in many compartments of the cell.


Apmis ◽  
1995 ◽  
Vol 103 (7-8) ◽  
pp. 869-877 ◽  
Author(s):  
JETTE M. BANGSBORG ◽  
PETER HINDERSSON ◽  
GEOFFREY SHAND ◽  
NIELS HØIBY

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