Saccharomyces cerevisiae amino acids sequence

Five structural genes for amino acid uptake systems have been cloned in Saccharomyces cerevisiae by functional complementation, and their putative amino acid sequences deduced from the respective nucleotide sequences (Fig. 2). 

Hamada, K., Terashima, H., Arisawa, M., and Kitada, K. (1998b). Amino acid sequence requirement for efficient incorporation of glycosylphosphtidylinositol-associated proteins into the cell wall of Saccharomyces cerevisiae. J. Biol. Chem. 273, 26946—26953. 

Figure 2. Histone H2A variants from yeast Saccharomyces cerevisiae S.c.), fruit fly Drosophila melanogaster D.m ), and human Homo sapiens H.s.). Two conserved domains distinguish H2A.Z-relatives (boxed regions amino acid sequences in the top). H2A.X possesses a conserved C-terminal stretch of four amino acids. The serine (red) becomes phosphorylated at sites of DNA damage. H2A ( Barr body-deficient ) and marcoH2A are present in mammals...

More recently, workers in Japan published the solution structure of yeast (Saccharomyces cerevisiae) apo-calmodulin (PDB ILKJ). Yeast calmodulin is 60% identical in its amino acid sequence with vertebrate CaMs. The ILKJ N-terminal domain with its two helix-loop-helix calcium-binding domains looks quite similar to those of IDMO and ICFD (see Figure 6.23). 

Berger, A. Schiltz, E. Schultz, G.E. Guanylate kinase from Saccharomyces cerevisiae. Isolation and characterization, crystallization and preliminary X-ray analysis, amino acid sequence and comparison with adenylate kinases. Eur. J. Biochem., 184, 433-443 (1989)... 

Fig. 10.3 Amino acid sequences of CuZn-SODs from various organisms.31 Yeast, Saccharomyces cerevisiae Neurospora, Neurospora crassa Arabido., Arabidopsis thaliana Cyt, cytosolic CuZn-SOD Chi, chloroplastic CuZn-SOD. Amino acid residue number is based on that of human CuZn-SOD. Residues conserved in all species are boxed.

Fig. 10.6 Amino acid sequences of Mn- and Fe-SODs. Yeast, Saccharomyces cerevisiae N. plumbagi., Nicotianaphimbaginifolia B. stearo., Bacillus stearothermophilus E. coli Escherichia coli A. thaliana, Arabiopsis thaliana-, P. ovalis, Pseudomonas ovalis. Residues conserved in Mn-SODsand/or Fe-SODs are boxed.

The membrane-bound archaeal ATPases have attracted considerable interest since patterns of inhibitor sensitivity, subunit structure, and amino-acid sequence homologies suggest a close relationship to the V-type ATPases [3,41]. In addition, the membrane-bound ATPases from S. acidocaldarius, H. salinarium (halobium), Methanosarcina barken, and the V-type ATPase from Saccharomyces cerevisiae are immunologically related [42]. 

Fig. 1. Elongation factor distance-matrix phylogenetic trees inferred from amino-acid sequence identities. Top phylogenetic tree inferred from EF-lcn/(EF-Tu) sequences. Bottom phylogenetic tree inferred from EF-2/(EF-G) sequences. Abbreviations Egr, Euglena gracilis See, Saccharomyces cerevisiae Asa, Artemia salina Dme, Drosophila melanogaster Hsa, Homo sapiens Eco, Escherichia coli Mlu, Micrococcus luteus Tma, Thermotoga maritima.

Fig. 4. Sequence alignment of flavocytochromes 62 and glycollate oxidase. The amino acid sequences of the mature forms of flavocytochromes 62 from Saccharomyces cerevisiae (Scb2) and Hansenula anomala (Hab2) and of glycollate oxidase from spinach (SpGO) are shown along with a consensus (Con) wherein all three sequences are identical. The interdomain hinge region and the proteinase-sensitive loop of flavocytochromes are boxed.

Lederer F, Simon AM, Verdiere J (1972) Saccharomyces cerevisiae iso-cytochromes c revision of the amino acid sequence between the cysteine residues. Biochem Biophys Res Commun 47 55-58... 

Fig. 3. Alignment of partial PCNA amino acid sequences from various model eukaryotic organisms. Shaded residues match the consensus. Sc, Saccharomyces cerevisiae, Sp, Schizosaccharomyces pombe. Dm, Drosophila melanogaster, Ce, Caenorhabditis elegans At, Arabidopsis thaliana Mm, Mus musculus Hs, Homo sapiens. Lysl27 and Lysl64 residues of S. cerevisiae (indicated with arrows) are modified by SUMO only, or Ub and SUMO, respectively.

Fig. 19. Alignment of homospermidine synthase (HSS) amino acid sequence from Senecio ver-nalis (Sv) in comparison to deoxyhypusine synthase amino acid sequences from six different species. Sv, Senecio vernalis Nt, Nicotiana tabacumi Hs, Homo sapiens Sc, Saccharomyces cerevisiae Nc, Neurospora crassa Mj, Methanococcus jannaschii. Black boxes denote identical amino acid residues in all seven sequences, framed boxes conservative replacement...

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