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- ****************************************************
- * Bacterial ice-nucleation proteins octamer repeat *
- ****************************************************
-
- Some gram-negative bacteria express proteins that enable them to promote the
- nucleation of ice at relatively high temperature (above -5 degree Celsius) [1,
- 2,3]. These proteins are localized at the surface of the outer membrane of the
- bacteria and can cause frost injury to many plant species. The primary
- structure of these ice-nucleation proteins is highly repetitive. A central
- repetitive domain represents about 80% of the total sequence. This domain is
- mainly formed by the repetition of a conserved region of forty eight residues
- (48-mer). The 48-mers are themselves composed of three blocks of 16 residues
- (16-mer). The first eight residues of each of these 16-mers are identical. It
- has been proposed that the repetitive domain may be directly responsible for
- aligning water molecules in the seed crystal.
-
- Schematic structure of a 48-mer region:
-
- [.........48.residues.repeated.domain..........]
- / / | | \ \
- AGYGSTxTagxxssli AGYGSTxTagxxsxlt AGYGSTxTaqxxsxlt
- [16.residues...] [16.residues...] [16.residues...]
-
- -Consensus pattern: A-G-Y-G-S-T-x-T
- -Sequences known to belong to this class detected by the pattern: ALL. This
- octamer sequence is found more than forty times in each of the known ice-
- nucleation proteins.
- -Other sequence(s) detected in SWISS-PROT: Paramecium primaurelia 168G surface
- protein (contains only one copy of the repeat).
- -Last update: June 1994 / Text revised.
-
- [ 1] Wolber P.K., Warren G.
- Trends Biochem. Sci. 14:179-182(1989).
- [ 2] Wolber P.K.
- Adv. Microb. Physiol. 34:205-237(1992).
- [ 3] Gurian-Sherman D., Lindow S.E.
- FASEB J. 7:1338-1343(1993).
-