scholarly journals The amino acid sequence of the cytochrome c2 from the phototrophic bacterium Rhodopseudomonas globiformis

1987 ◽  
Vol 246 (1) ◽  
pp. 115-120 ◽  
Author(s):  
R P Ambler ◽  
T E Meyer ◽  
M A Cusanovich ◽  
M D Kamen
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sequence Similarity ◽  
British Library ◽  
Sequence Information ◽  
Cytochrome C2 ◽  
Percentage Sequence Identity ◽  
Acidophilic Bacterium ◽  
High Degree ◽  
Rhodopseudomonas Globiformis

The amino acid sequence of the principal soluble cytochrome c from the phototrophic acidophilic bacterium Rhodopseudomonas (or Rhodopila) globiformis was determined. By the criteria of percentage sequence identity and fewness of internal insertions and deletions it is more similar in sequence to some mitochondrial cytochromes c than to any known bacterial cytochrome. The organism does not have any properties that commend it as being particularly similar to postulated prokaryotic precursors of the mitochondrion. We consider that the relatively high degree of sequence similarity is an instance of convergence, and is an example of the limitations that are imposed on attempts to deduce distant evolutionary relationships from sequence information. Detailed evidence for the amino acid sequence of the protein has been deposited as Supplementary Publication SUP 50136 (12 pages) at the British Library Lending Division, Boston Spa, West Yorkshire LS23 7BQ, U.K., from whom copies are available on prepayment [see Biochem. J. (1987) 241, 5].

scholarly journals Type II intermediate-filament proteins from wool. The amino acid sequence of component 5 and comparison with component 7c

1992 ◽  
Vol 282 (1) ◽  
pp. 291-297 ◽  
Author(s):  
L G Sparrow ◽  
C P Robinson ◽  
J Caine ◽  
D T W McMahon ◽  
P M Strike
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Intermediate Filament ◽  
Sequence Similarity ◽  
British Library ◽  
Intermediate Filament Protein ◽  
Type Ii ◽  
Blocking Group ◽  
Intermediate Filament Proteins ◽  
Merino Wool

Component 5 is one of the four type II intermediate-filament proteins found in the hard keratin wool. It was isolated as the S-carboxymethyl derivative from Merino wool and its amino acid sequence was determined by manual and automatic sequencing of peptides produced by chemical and enzymic cleavage. Component 5 is an N-terminally blocked molecule of 503 residues and Mr (not including the blocking group) of 56,600. The blocking group has not been identified. The amino acid sequence of component 5 shows 77% sequence identity with that of component 7c, another type II wool intermediate-filament protein [Sparrow, Robinson, McMahon & Rubira (1989) Biochem. J. 261, 1015-1022]. The sequence similarity extends from the N-termini of the two molecules to residue 459 (component 5 sequence); however, there is no recognizable sequence similarity in the remaining C-terminal 43 amino acid residues. Details of procedures used in determining the sequence of component 5 have been deposited as a Supplementary Publication SUP 50168 (80 pages) at the British Library Document Supply Centre, Boston Spa, Wetherby, West Yorkshire, LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1992) 281, 5. The information comprises: (1) details of chemical and enzymic methods used for cleavage of component 5, peptide CN1, the peptide mixture CN2/3 and various other peptides, (2) details of the procedures used for the fractionation and purification of peptides from (1), including Figures showing the elution profiles from the chromatographic steps used, and (3) details of the method used to determine the C-terminal sequence of component 5.

scholarly journals Comparison of the Antibacterial Properties of Phage Endolysins SAL-1 and LysK

2011 ◽  
Vol 55 (4) ◽  
pp. 1764-1767 ◽  
Author(s):  
Soo Youn Jun ◽  
Gi Mo Jung ◽  
Jee-Soo Son ◽  
Seong Jun Yoon ◽  
Yun-Jaie Choi ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Cell Wall ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Enzymatic Activity ◽  
Bacterial Cell ◽  
Sequence Similarity ◽  
Antibacterial Properties ◽  
Amino Acid Sequence Similarity ◽  
High Degree

ABSTRACTIn spite of the high degree of amino acid sequence similarity between the newly discovered phage endolysin SAL-1 and the phage endolysin LysK, SAL-1 has an approximately 2-fold-lower MIC against severalStaphylococcus aureusstrains and higher bacterial cell-wall-hydrolyzing activity than LysK. The amino acid residue change contributing the most to this enhanced enzymatic activity is a change from glutamic acid to glutamine at the 114th residue.

C-Terminal amino acid sequence of chicken pepsinogen and its homology with sequences of other acid proteases

1980 ◽  
Vol 45 (4) ◽  
pp. 1144-1154 ◽  
Author(s):  
Miroslav Baudyš ◽  
Helena Keilová ◽  
Vladimír Kostka
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
The Other ◽  
Terminal Sequence ◽  
Terminal Part ◽  
Terminal Amino Acid ◽  
Tryptic Peptides ◽  
Terminal Amino ◽  
High Degree ◽  
Terminal Amino Acid Sequence

To determine the primary structure of the C-terminal part of the molecule of chicken pepsinogen the tryptic, chymotryptic and thermolytic digest of the protein were investigated and peptides derived from this region were sought. These peptides permitted the following 21-residue C-terminal sequence to be determined: ...Ile-Arg-Glu-Tyr-Tyr-Val-Ile-Phe-Asp-Arg-Ala-Asn-Asn-Lys-Val-Gly-Leu-Ser-Pro-Leu-Ser.COOH. A comparison of this structure with the C-terminal sequential regions of the other acid proteases shows a high degree of homology between chicken pepsinogen and these proteases (e.g., the degree of homology with respect to hog pepsinogen and calf prochymosin is about 66%). Additional tryptic peptides, derived from the N-terminal part of the zymogen molecule whose amino acid sequence has been reported before, were also obtained in this study. This sequence was extended by two residues using an overlapping peptide. An ancillary result of this study was the isolation of tryptic peptides derived from other regions of the zymogen molecule.

The amino acid sequence of yeast phosphoglycerate mutase

1982 ◽  
Vol 215 (1198) ◽  
pp. 19-44 ◽  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Proteolytic Enzymes ◽  
Phosphoglycerate Mutase ◽  
Crystallographic Structure ◽  
X Ray ◽  
C Terminus ◽  
Detailed Interpretation ◽  
High Degree

The complete amino acid sequence of yeast phosphoglycerate mutase comprising 241 residues has been determined. The sequence was deduced from the two cyanogen bromide fragments, and from the peptides derived from these fragments after digestion by a number of proteolytic enzymes. Determination of this sequence now allows a detailed interpretation of the existing high-resolution X-ray crystallographic structure. A comparison of the sequence reported here with the sequences of peptides from phosphoglycerate mutases from other species, and with the sequence of erythrocyte diphosphoglycerate mutase, indicates that these enzymes have a high degree of structural homology. Autolysis of phosphoglycerate mutase by yeast extracts leads to the complete loss of mutase activity, and the formation of electrophoretically distinguishable forms (R. Sasaki, E. Sugimoto & H. Chiba, Archs Biochem. Biophys. 115, 53-61 (1966)). It is apparent from the amino acid sequence that these changes are due to the loss of an 8─12 residue peptide from the C-terminus.

scholarly journals The complete amino acid sequence of three alcohol dehydrogenase alleloenzymes (AdhN-11, AdhS and AdhUF) from the fruitfly Drosophila melanogaster

1980 ◽  
Vol 187 (3) ◽  
pp. 875-883 ◽  
Author(s):  
D R Thatcher
Keyword(s):  
Drosophila Melanogaster ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Alcohol Dehydrogenase ◽  
Aspartic Acid ◽  
Structure Prediction ◽  
Secondary Structure Prediction ◽  
British Library ◽  
Horse Liver ◽  
And Staphylococcus Aureus

The sequence of three alcohol dehydrogenase alleloenzymes from the fruitfly Drosophila melanogaster has been determined by the sequencing of peptides produced by trypsin, chymotrypsin, thermolysin, pepsin and Staphylococcus aureus-V8-proteinase digestion. The amino acid sequence shows no obvious homology with the published sequences of the horse liver and yeast enzymes, and secondary structure prediction suggests that the nucleotide-binding domain is located in the N-terminal half of the molecule. The amino acid substitutions between AdhN-11 (a point mutation of AdhF), AdhS and AdhUF alleloenzymes were identified. AdhN-11 alcohol dehydrogenase differed from the other two by a glycine-14-(AdhS and AdhUF)-to-aspartic acid substitution, the AdhS enzyme from AdhN-11 and AdhUF enzymes by a threonine-192-(AdhN-11 and AdhUF)-to-lysine (AdhS) substitution and the AdhUF enzyme was found to differ by an alanine-45-(AdhS and AdhN-11)-to-aspartic acid (AdhUF) charge substitution and a ‘silent’ asparagine-8-(AdhS and AdhN-11)-to-alanine (AdhUF) substitution. Detailed sequence evidence has been deposited as Supplementary Publication SUP 50107 (36 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1978) 169, 5.

scholarly journals Engineered Resistance Against Papaya ringspot virus in Venezuelan Transgenic Papayas

Plant Disease ◽  
2004 ◽  
Vol 88 (5) ◽  
pp. 516-522 ◽  
Author(s):  
Gustavo Fermin ◽  
Valentina Inglessis ◽  
Cesar Garboza ◽  
Sairo Rangel ◽  
Manuel Dagert ◽  
...  
Keyword(s):  
Amino Acid ◽  
Agrobacterium Tumefaciens ◽  
Coat Protein ◽  
Amino Acid Sequence ◽  
Sequence Similarity ◽  
Ringspot Virus ◽  
Amino Acid Sequence Similarity ◽  
Papaya Ringspot Virus ◽  
Local Varieties ◽  
Cp Gene

Local varieties of papaya grown in the Andean foothills of Mérida, Venezuela, were transformed independently with the coat protein (CP) gene from two different geographical Papaya ringspot virus (PRSV) isolates, designated VE and LA, via Agrobacterium tumefaciens. The CP genes of both PRSV isolates show 92 and 96% nucleotide and amino acid sequence similarity, respectively. Four PRSV-resistant R0 plants were intercrossed or selfed, and the progenies were tested for resistance against the homologous isolates VE and LA, and the heterologous isolates HA (Hawaii) and TH (Thailand) in greenhouse conditions. Resistance was affected by sequence similarity between the transgenes and the challenge viruses: resistance values were higher for plants challenged with the homologous isolates (92 to 100% similarity) than with the Hawaiian (94% similarity) and, lastly, Thailand isolates (88 to 89% similarity). Our results show that PRSV CP gene effectively protects local varieties of papaya against homologous and heterologous isolates of PRSV.

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