Analysis of Distributions of Amino Acids in the Primary Structure of Apoptosis Regulator Bcl-2 Family According to the Random Mechanism

2002 ◽  
Vol 6 (6) ◽  
pp. 407-414 ◽  
Author(s):  
Guang Wu ◽  
Shaomin Yan
Keyword(s):  
Amino Acids ◽  
Primary Structure ◽  
Random Mechanism

scholarly journals The primary structure of NG2, a novel membrane-spanning proteoglycan.

1991 ◽  
Vol 114 (2) ◽  
pp. 359-371 ◽  
Author(s):  
A Nishiyama ◽  
K J Dahlin ◽  
J T Prince ◽  
S R Johnstone ◽  
W B Stallcup
Keyword(s):  
Amino Acids ◽  
Chondroitin Sulfate ◽  
Primary Structure ◽  
Disulfide Bonds ◽  
Transmembrane Domain ◽  
Core Protein ◽  
Extracellular Domain ◽  
Cdna Clones ◽  
Amino Terminal ◽  
Extracellular Region

The complete primary structure of the core protein of rat NG2, a large, chondroitin sulfate proteoglycan expressed on O2A progenitor cells, has been determined from cDNA clones. These cDNAs hybridize to an mRNA species of 8.9 kbp from rat neural cell lines. The total contiguous cDNA spans 8,071 nucleotides and contains an open reading frame for 2,325 amino acids. The predicted protein is an integral membrane protein with a large extracellular domain (2,224 amino acids), a single transmembrane domain (25 amino acids), and a short cytoplasmic tail (76 amino acids). Based on the deduced amino acid sequence and immunochemical analysis of proteolytic fragments of NG2, the extracellular region can be divided into three domains: an amino terminal cysteine-containing domain which is stabilized by intrachain disulfide bonds, a serine-glycine-containing domain to which chondroitin sulfate chains are attached, and another cysteine-containing domain. Four internal repeats, each consisting of 200 amino acids, are found in the extracellular domain of NG2. These repeats contain a short sequence that resembles the putative Ca(++)-binding region of the cadherins. The sequence of NG2 does not show significant homology with any other known proteins, suggesting that NG2 is a novel species of integral membrane proteoglycan.

scholarly journals Sequence of the N-terminal half of Bacillus amyloliquefaciens α-amylase

1980 ◽  
Vol 185 (2) ◽  
pp. 387-395 ◽  
Author(s):  
H Chung ◽  
F Friedberg
Keyword(s):  
Amino Acids ◽  
Bacillus Subtilis ◽  
Amino Acid ◽  
Aspartic Acid ◽  
Primary Structure ◽  
Bacillus Amyloliquefaciens ◽  
Proteolytic Enzymes ◽  
Alpha Amylase ◽  
Sequence Determination ◽  
N Terminus

Bacillus amyloliquefaciens alpha-amylase (1,4-alpha-D-glucan glucanohydrolase. EC 3.2.1.1), which is commercially supplied as ‘Bacillus subtilis alpha-amylase’ does not cross-react immunologically with B. subtilis alpha-amylase. This enzyme (from B. amyloliquefaciens) was cleaved by treatment with CNBr into seven fragments. Peptide A was selected for sequence determination. It is the longest one, containing 185 amino acids (i.e. approx. 50% of the total molecule) and connects to the hexapeptide of the N-terminus. Its primary structure was aligned by use of various proteolytic enzymes. The sequence of amino acids 181-184 is identical with that of amino acids 14-17 of the alpha-amylase isolated from B. subtilis (except that amino acid 183 is asparagine rather than aspartic acid).

scholarly journals Sulfide-Quinone Reductase from Rhodobacter capsulatus: Requirement for Growth, Periplasmic Localization, and Extension of Gene Sequence Analysis

1999 ◽  
Vol 181 (20) ◽  
pp. 6516-6523 ◽  
Author(s):  
Michael Schütz ◽  
Iris Maldener ◽  
Christoph Griesbeck ◽  
Günter Hauska
Keyword(s):  
Amino Acids ◽  
Sequence Analysis ◽  
Primary Structure ◽  
Gene Sequence ◽  
Rhodobacter Capsulatus ◽  
Quinone Reductase ◽  
Open Reading Frames ◽  
Fusion Construct ◽  
Periplasmic Localization ◽  
Reading Frames

ABSTRACT The entire sequence of the 3.5-kb fragment of genomic DNA fromRhodobacter capsulatus which contains the sqrgene and a second complete and two further partial open reading frames has been determined. A correction of the previously publishedsqr gene sequence (M. Schütz, Y. Shahak, E. Padan, and G. Hauska, J. Biol. Chem. 272:9890–9894, 1997) which in the deduced primary structure of the sulfide-quinone reductase changes four positive into four negative charges and the number of amino acids from 425 to 427 was necessary. The correction has no further bearing on the former sequence analysis. Deletion and interruption strains document that sulfide-quinone reductase is essential for photoautotrophic growth on sulfide. The sulfide-oxidizing enzyme is involved in energy conversion, not in detoxification. Studies with an alkaline phosphatase fusion protein reveal a periplasmic localization of the enzyme. Exonuclease treatment of the fusion construct demonstrated that the C-terminal 38 amino acids of sulfide-quinone reductase were required for translocation. An N-terminal signal peptide for translocation was not found in the primary structure of the enzyme. The possibility that the neighboring open reading frame, which contains a double arginine motif, may be involved in translocation has been excluded by gene deletion (rather, the product of this gene functions in an ATP-binding cassette transporter system, together with the product of one of the other open reading frames). The results lead to the conclusion that the sulfide-quinone reductase of R. capsulatus functions at the periplasmic surface of the cytoplasmic membrane and that this flavoprotein is translocated by a hitherto-unknown mechanism.

Die primäre Proteinstruktur von Stämmen des Tabakmosaikvirus

1969 ◽  
Vol 24 (7) ◽  
pp. 870-877 ◽  
Author(s):  
J. Jauregui-Adell ◽  
I. Hindennach ◽  
H. G. Wittmann
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Coat Protein ◽  
Tobacco Mosaic Virus ◽  
Primary Structure ◽  
Amino Acid Sequences ◽  
The Other ◽  
Protein Subunit ◽  
Tryptic Peptides ◽  
Tmv Strains

The sequence of amino acids within the coat protein of the strain Holmes rib grass of tobacco mosaic virus (TMV) has been determined. In this communication the amino acid compositions of the coat protein and of all tryptic peptides are reported. Furthermore the experimental details are given for the elucidation of the amino acid sequences within the first three tryptic peptides, containing 61 amino acids.It has been found that the strain Holmes rib grass differs very extensively in the primary structure from the other TMV strains whose sequences are known. It differs from each of the other strains in more than 50% of the amino acid positions and it contains two amino acids less per protein subunit than the other TMV strains.

scholarly journals The Fusion Protein Specificity of the Parainfluenza Virus Hemagglutinin-Neuraminidase Protein Is Not Solely Defined by the Primary Structure of Its Stalk Domain

2015 ◽  
Vol 89 (24) ◽  
pp. 12374-12387 ◽  
Author(s):  
Masato Tsurudome ◽  
Morihiro Ito ◽  
Junpei Ohtsuka ◽  
Kenichiro Hara ◽  
Hiroshi Komada ◽  
...  
Keyword(s):  
Amino Acids ◽  
Fusion Protein ◽  
Primary Structure ◽  
Specific Interaction ◽  
Simian Virus ◽  
Fusion Event ◽  
F Protein ◽  
Protein Specificity ◽  
Head Domain ◽  
Stalk Domain

ABSTRACTVirus-specific interaction between the attachment protein (HN) and the fusion protein (F) is prerequisite for the induction of membrane fusion by parainfluenza viruses. This HN-F interaction presumably is mediated by particular amino acids in the HN stalk domain and those in the F head domain. We found in the present study, however, that a simian virus 41 (SV41) F-specific chimeric HPIV2 HN protein, SCA, whose cytoplasmic, transmembrane, and stalk domains were derived from the SV41 HN protein, could not induce cell-cell fusion of BHK-21 cells when coexpressed with an SV41 HN-specific chimeric PIV5 F protein, no. 36. Similarly, a headless form of the SV41 HN protein failed to induce fusion with chimera no. 36, whereas it was able to induce fusion with the SV41 F protein. Interestingly, replacement of 13 amino acids of the SCA head domain, which are located at or around the dimer interface of the head domain, with SV41 HN counterparts resulted in a chimeric HN protein, SCA-RII, which induced fusion with chimera no. 36 but not with the SV41 F protein. More interestingly, retroreplacement of 11 out of the 13 amino acids of SCA-RII with the SCA counterparts resulted in another chimeric HN protein, IM18, which induced fusion either with chimera no. 36 or with the SV41 F protein, similar to the SV41 HN protein. Thus, we conclude that the F protein specificity of the HN protein that is observed in the fusion event is not solely defined by the primary structure of the HN stalk domain.IMPORTANCEIt is appreciated that the HN head domain initially conceals the HN stalk domain but exposes it after the head domain has bound to the receptors, which allows particular amino acids in the stalk domain to interact with the F protein and trigger it to induce fusion. However, other regulatory roles of the HN head domain in the fusion event have been ill defined. We have shown in the current study that removal of the head domain or amino acid substitutions in a particular region of the head domain drastically change the F protein specificity of the HN protein, suggesting that the ability of a given HN protein to interact with an F protein is defined not only by the primary structure of the HN stalk domain but also by its conformation. This notion seems to account for the unidirectional substitutability among rubulavirus HN proteins in triggering noncognate F proteins.

Sign in / Sign up

Export Citation Format

Share Document