Sequence analysis of a 33·1 kb fragment from the left arm of Saccharomyces cerevisiae chromosome X, including putative proteins with leucine zippers, a fungal Zn(II)2‐Cys6 binuclear cluster domain and a putative α2‐SCB‐α2 binding site

Miosga, Thomas; Schaaff-Gerstenschläger, Ine; Chalwatzis, N.; Baur, Axel; Boles, Eckhard; Fournier, Claire T.; Schmitt, Sarah; Velten, C.; Wilhelm, Nicole; Zimmermann, Friedrich K.

doi:10.1002/yea.320110709

Cited by 22 publications

(14 citation statements)

References 56 publications

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“…Insect, fungus and plant proteins had been identified earlier as belonging to the CRISP superfamily (Morrissette et al, 1995). New database searches have now revealed that, in addition, a hookworm protein called ancylostoma secreted protein (GenBank entry U26187), a hypothetical C. elegans protein (GenBank entry U23514, gene F48E8.1; Wilson et al, 1994) and three hypothetical yeast proteins, one encoded on chromosome XI (SWISSPROT entry YKZ3XYEAST; Dujon et al, 1994) and two on chromosome X (GenBank entry X83502, genes 51022 and 51027; Miosga et al, 1995) are also members of the same superfamily. None of these proteins has however the complete cysteine-rich C-terminal domain characteristic of the CRISP family.…”

Section: Resultsmentioning

confidence: 99%

The Human Cysteine‐Rich Secretory Protein (CRISP) Family

Krätzschmar¹,

Haendler²,

Eberspaecher³

et al. 1996

European Journal of Biochemistry

198

145

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We report the isolation and characterisation of cDNAs encoding three different, human members of the cysteine-rich secretory protein (CRISP) family. The novel CRISP-I exists in five cDNA subtypes differing by the presence or absence of a stretch coding for a C-terminal cysteine-rich domain so far found in all members of the family, and by the length of their 3'-untranslated region. CRISP-2 cDNA corresponds to the previously described TPXI form, with so far unreported 5'-untranslated sequence heterogeneities while CRISP-3 cDNA codes for a new, unique protein. Northern blot analysis of various human organs indicates that CRISP-1 transcripts are epididymis-specific whereas CRISP-2ITPXI transcripts are detected mainly in the testis and also in the epididymis. CRISP-3 transcripts are more widely distributed and found predominantly in the salivary gland, pancreas and prostate, and in less abundance in the epididymis, ovary, thymus and colon. A protein reacting with an anti-mouse CRISP-I antibody was isolated from human epididymal extracts and N-terminal sequencing revealed that it corresponded to the CRISP-I cDNA we have isolated. In contrast to findings on its rat counterpart epididymal protein DE/acidjc epididymal glycoprotein (AEG), no significant association of CRISP-1 with human spermatozoa was observed.

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Section: Resultsmentioning

confidence: 99%

The Human Cysteine‐Rich Secretory Protein (CRISP) Family

Krätzschmar¹,

Haendler²,

Eberspaecher³

et al. 1996

European Journal of Biochemistry

198

145

View full text Add to dashboard Cite

show abstract

“…Structural analysis of tablysin-15 revealed a hydrophobic channel that binds leukotrienes with sub-micromolar affi nities, indicating that the protein functions as an anti-infl ammatory scavenger of eicosanoids ( 20 ). GLIPR2, on the other hand, is the smallest of the mammalian CAP proteins, and the one most closely related to yeast Pry1 ( 26 ). It is highly expressed in the tumor glioblastoma multiform, which arises from brain immune cells and accounts for over 65% of all human primary brain tumors (27)(28)(29).…”

Section: Discussionmentioning

confidence: 99%

The caveolin-binding motif of the pathogen-related yeast protein Pry1, a member of the CAP protein superfamily, is required for in vivo export of cholesteryl acetate

Choudhary

Darwiche

Gfeller

et al. 2014

Journal of Lipid Research

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including immune defense in mammals and plants, pathogen virulence, sperm maturation and fertilization, venom toxicity, and prostate and brain cancer. Named after the founding members of this protein superfamily (cysteine-rich secretory protein, antigen 5, and pathogenesis-related 1), the CAP superfamily comprises more than 4,500 members in over 1,500 species, and family members are present in all kingdoms of life. Almost all CAP proteins are secreted glycoproteins and they are stable in the extracellular space over a wide range of conditions. All members of this superfamily share a common CAP domain of approximately 150 amino acids, which adopts a unique ␣ -␤ -␣ sandwich fold. The structural conservation of this domain suggests that CAP proteins exert a fundamentally similar function. The molecular mode of action of the CAP proteins, however, has remained enigmatic [for reviews see ( 1, 2 )].CAP proteins share limited sequence identity with each other and are characterized by two PROSITE-recognized sequence motifs, referred to as the CRISP family signature (shaded boxes in Fig. 1 ). An early comparison of the structure of the plant pathogenesis-related protein (PR)-1 with that of the human glioma pathogenesis-related protein 1 (GLIPR1) revealed that the small and structurally conserved 17-21 kDa CAP domain adopts a unique ␣ -␤ -␣ sandwich fold, in which a three-stranded anti-parallel ␤ -sheet is fl anked by three helices on one side, and a fourth helix on the other ( 3 ). This three-stacked layer is stabilized by hydrophobic interactions, multiple hydrogen bonds, and by two highly conserved disulfi de bonds. These features are thought to provide the thermal, pH, and proteolytic stability required for the extracellular function of these proteins ( 3, 4 ). The CAP domain harbors four highly 28 February 2014. Published, JLR Papers in Press, March 5, 2014 DOI 10.1194 The caveolin-binding motif of the pathogen-related yeast protein Pry1, a member of the CAP protein superfamily, is required for in vivo export of cholesteryl acetate Abbreviations: DOPE, discrete optimized protein energy; GLIPR1, glioma pathogenesis-related protein 1; PR, pathogenesis-related protein; OD, optical density; PDB, protein data base; Pry, pathogen-related yeast; RMSD, root mean square deviation; SC, synthetic complete. Manuscript received 15 January 2014 and in revised form

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“…Sequences from Saccharomyces cere isiae were determined in the framework of the EU BIOTECH project for sequencing the yeast genome. It was noted that the proteins share a weak similarity with the serine\threonine-rich protein Aga1p, which mediates cell surface attachment of the yeast cell adhesion glycoprotein a-agglutinin [48].…”

Section: Comparative Analysis Of Pr-1 Type Proteinsmentioning

confidence: 99%