Purification, properties, and N-terminal amino acid sequence of certain 50S ribosomal subunit proteins from the archaebacterium Halobacterium cutirubrum

1984 ◽  
Vol 62 (6) ◽  
pp. 426-433 ◽  
Author(s):  
Alastair T. Matheson ◽  
Makoto Yaguchi ◽  
Patricia Christensen ◽  
C. Fernand Rollin ◽  
Sadiq Hasnain
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sequence Homology ◽  
Ribosomal Proteins ◽  
Large Subunit ◽  
Ribosomal Subunit ◽  
Terminal Amino Acid ◽  
Terminal Amino ◽  
Terminal Amino Acid Sequence

Sixteen ribosomal proteins (r-proteins) from the 50S ribosomal subunit of the archaebacterium Halobacterium cutirubrum have been purified and their amino acid composition and partial N-terminal amino acid sequence have been determined. These proteins as a group are much more acidic than the large subunit r-proteins from eubacteria or eukaryotes. Little sequence homology is evident between the 50S subunit archaebacterial r-proteins and the equivalent proteins from the eubacterium Escherichia coli.

scholarly journals The overexpression and complete amino acid sequence of Escherichia coli 3-dehydroquinase

1986 ◽  
Vol 238 (2) ◽  
pp. 475-483 ◽  
Author(s):  
K Duncan ◽  
S Chaudhuri ◽  
M S Campbell ◽  
J R Coggins
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Polypeptide Chain ◽  
Amino Acid Residues ◽  
Transcript Mapping ◽  
Terminal Amino Acid ◽  
Terminal Amino ◽  
Terminal Amino Acid Sequence

The enzyme 3-dehydroquinase was purified in milligram quantities from an overproducing strain of Escherichia coli. The amino acid sequence was deduced from the nucleotide sequence of the aroD gene and confirmed by determining the amino acid composition of the overproduced enzyme and its N-terminal amino acid sequence. The complete polypeptide chain consists of 240 amino acid residues and has a calculated subunit Mr of 26,377. Transcript mapping revealed that aroD is a typical monocistronic gene.

N-terminal amino acid sequence homology of storage protein components from barley and a diploid wheat

Nature ◽  
1980 ◽  
Vol 286 (5772) ◽  
pp. 520-522 ◽  
Author(s):  
Peter R. Shewry ◽  
Jean-Claude Autran ◽  
Charles C. Nimmo ◽  
Ellen J.-L. Lew ◽  
Donald D. Kasarda
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sequence Homology ◽  
Storage Protein ◽  
Diploid Wheat ◽  
Amino Acid Sequence Homology ◽  
Terminal Amino Acid ◽  
Terminal Amino ◽  
Protein Components ◽  
Terminal Amino Acid Sequence

scholarly journals Cloning of a Beta-Hemolysin Gene ofBrachyspira (Serpulina) hyodysenteriaeand Its Expression in Escherichia coli

2001 ◽  
Vol 69 (2) ◽  
pp. 706-711 ◽  
Author(s):  
Tsungda Hsu ◽  
David L. Hutto ◽  
F. Chris Minion ◽  
Richard L. Zuerner ◽  
Michael J. Wannemuehler
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Gene Sequence ◽  
Binding Motif ◽  
Terminal Amino Acid ◽  
Hemolytic Toxin ◽  
Terminal Amino ◽  
Cloned Gene ◽  
Terminal Amino Acid Sequence

ABSTRACT Brachyspira (Serpulina)hyodysenteriae induces a mucohemorrhagic diarrheal disease in pigs. The production of a beta-hemolysin has been considered a major virulence attribute of this organism. Previous reports have failed to correlate a specific cloned gene sequence with a purified beta-hemolytic protein sequence. Thus, questions still remain concerning the structural gene sequence of the hemolysin. To answer this question unequivocally, the beta-hemolytic toxin was purified from extracts of log-phase spirochetes, and the N-terminal amino acid sequence was determined (K-D-V-V-A-N-Q-L-N-I-S-D-K) and compared with the translated sequences of previously cloned genes, tlyAto tlyC. The lack of homology between tlyA totlyC translated sequences and the purified beta-hemolytic toxin sequence resulted in the study that is reported here. A degenerate probe was designed based on the N-terminal amino acid sequence of the purified beta-hemolysin and used to screen a B. hyodysenteriae genomic library. Three overlapping clones were identified, and one was sequenced to reveal an open reading frame coding for a putative 8.93-kDa polypeptide containing the N-terminal sequence of the purified beta-hemolysin. To distinguish this gene from the tlyA to tlyC genes, it has been designatedhlyA. A hemolysis-negative Escherichia colistrains containing hlyA was beta-hemolytic on blood agar media. Also, the hemolytic activity of the recombinant protein had identical protease and lipase sensitivities and electrophoretic mobility to those of native B. hyodysenteriaebeta-hemolysin. Based on sequence analysis, the translated protein had a pI of 4.3, an α-helical structure, and a phosphopantetheine binding motif. Hybridization analysis of genomic DNA indicated that thehlyA gene was present in B. hyodysenteriae andB. intermedia but was not detected in B. innocens, B. pilosicoli, or B. murdochiiunder high-stringency conditions. The location of hlyA on the chromosomal map was distinct from the locations oftlyA, tlyB, and tlyC.

scholarly journals Purification, N-terminal amino acid sequence and properties of hydroxymethylbilane synthase (porphobilinogen deaminase) from Escherichia coli

1986 ◽  
Vol 240 (1) ◽  
pp. 273-276 ◽  
Author(s):  
G J Hart ◽  
C Abell ◽  
A R Battersby
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Porphobilinogen Deaminase ◽  
Terminal Amino Acid ◽  
Ph Values ◽  
Apparent Homogeneity ◽  
Terminal Amino ◽  
Ionizable Groups ◽  
Terminal Amino Acid Sequence

Hydroxymethylbilane synthase (porphobilinogen deaminase) was purified to apparent homogeneity from Escherichia coli. The enzyme is a monomer of Mr approx. 40,000. The Km for porphobilinogen and relative Vmax. values have been obtained at various pH values over the range 6.2-8.8, enabling pK values for ionizable groups important for activity to be determined. The N-terminal amino acid sequence is presented.

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