Structural highlights
Function
[FLO1_YEAST] Cell wall protein that participates directly in adhesive cell-cell interactions during yeast flocculation, a reversible, asexual and Ca(2+)-dependent process in which cells adhere to form aggregates (flocs) consisting of thousands of cells. The lectin-like protein sticks out of the cell wall of flocculent cells and selectively binds mannose residues in the cell walls of adjacent cells. Activity is inhibited by mannose, but not by glucose, maltose, sucrose or galactose. Also involved in cell-substrate adhesion.[1] [2] [3] [4]
Publication Abstract from PubMed
Flo1p and Lg-Flo1p are two cell-wall adhesins belonging to the Flo (flocculation) protein family from the yeasts Saccharomyces cerevisiae and S. pastorianus. The main function of these modular proteins endowed with calcium-dependent lectin activity is to mediate cell-cell adhesion events during yeast flocculation, a process which is well known at the cellular level but still not fully characterized from a molecular perspective. Recently, structural features of the N-terminal Flo lectin domains, including the N-terminal domain of Lg-Flo1p (N-Lg-Flo1p), and their interactions with carbohydrate molecules have been investigated. However, structural data concerning the N-terminal domain of Flo1p (N-Flo1p), which is the most specific among the Flo proteins, are missing and information about the N-Lg-Flo1p-carbohydrate interaction still lacks detailed structural insight. Here, the crystallization and preliminary X-ray characterization of the apo form and the mannose complex of N-Flo1p and X-ray analysis of N-Lg-Flo1p crystals soaked in alpha-1,2-mannobiose are reported. The N-Flo1p crystals diffracted to a resolution of 1.43 A in the case of the apo form and to 2.12 A resolution for the mannose complex. Both crystals were orthorhombic and belonged to space group P212121, with one molecule in the asymmetric unit. The N-Lg-Flo1p-alpha-1,2-mannobiose complex crystal diffracted to 1.73 A resolution and belonged to the monoclinic space group P1211 with two molecules in the asymmetric unit.
The mannose-specific lectin domains of Flo1p from Saccharomyces cerevisiae and Lg-Flo1p from S. pastorianus: crystallization and preliminary X-ray diffraction analysis of the adhesin-carbohydrate complexes.,Ielasi FS, Goyal P, Sleutel M, Wohlkonig A, Willaert RG Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jul;69(Pt 7):779-82. doi: , 10.1107/S1744309113015030. Epub 2013 Jun 28. PMID:23832207[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fichtner L, Schulze F, Braus GH. Differential Flo8p-dependent regulation of FLO1 and FLO11 for cell-cell and cell-substrate adherence of S. cerevisiae S288c. Mol Microbiol. 2007 Dec;66(5):1276-89. PMID:18001350 doi:http://dx.doi.org/MMI6014
- ↑ Kobayashi O, Hayashi N, Kuroki R, Sone H. Region of FLO1 proteins responsible for sugar recognition. J Bacteriol. 1998 Dec;180(24):6503-10. PMID:9851992
- ↑ Bony M, Barre P, Blondin B. Distribution of the flocculation protein, flop, at the cell surface during yeast growth: the availability of flop determines the flocculation level. Yeast. 1998 Jan 15;14(1):25-35. PMID:9483793 doi:<25::AID-YEA197>3.0.CO;2-C http://dx.doi.org/10.1002/(SICI)1097-0061(19980115)14:1<25::AID-YEA197>3.0.CO;2-C
- ↑ Guo B, Styles CA, Feng Q, Fink GR. A Saccharomyces gene family involved in invasive growth, cell-cell adhesion, and mating. Proc Natl Acad Sci U S A. 2000 Oct 24;97(22):12158-63. PMID:11027318 doi:http://dx.doi.org/10.1073/pnas.220420397
- ↑ Ielasi FS, Goyal P, Sleutel M, Wohlkonig A, Willaert RG. The mannose-specific lectin domains of Flo1p from Saccharomyces cerevisiae and Lg-Flo1p from S. pastorianus: crystallization and preliminary X-ray diffraction analysis of the adhesin-carbohydrate complexes. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jul;69(Pt 7):779-82. doi: , 10.1107/S1744309113015030. Epub 2013 Jun 28. PMID:23832207 doi:http://dx.doi.org/10.1107/S1744309113015030
