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- *************************************************
- * Ribonuclease T2 family histidine active sites *
- *************************************************
-
- The fungal ribonucleases T2 from Aspergillus oryzae, M from Aspergillus saitoi
- and Rh from Rhizopeus niveus are structurally and functionally related 30 Kd
- glycoproteins [1] that cleave the 3'-5' internucleotide linkage of RNA via a
- nucleotide 2',3'-cyclic phosphate intermediates (EC 3.1.27.1).
-
- A number of other RNAses have been found to be evolutionary related to these
- fungal enzymes:
-
- - Self-incompatibility [2] in flowering plants is often controlled by a
- single gene (S-gene) that has several alleles. This gene prevents
- fertilization by self-pollen or by pollen bearing either of the two S-
- alleles expressed in the style. The self-incompatibility glycoprotein from
- several higher plants of the solanaceae family has been shown [2,3] to be
- a ribonuclease.
- - Phosphate-starvation induced RNAses LE and LX from tomato [4]. These two
- enzymes are probably involved in a phosphate-starvation rescue system.
- - Escherichia coli periplasmic RNAse I (EC 3.1.27.6) (gene rna) [5].
-
- Two histidines residues have been shown [6,7] to be involved in the catalytic
- mechanism of RNase T2 and Rh. These residues and the region around them are
- highly conserved in all the sequence described above. We have developed two
- signature patterns, one for each of the two active-site histidines. The
- second pattern also contains a cysteine which is known to be involved in a
- disulfide bond.
-
- -Consensus pattern: [FYWL]-x-[LIVM]-H-G-L-W-P
- [H is an active site residue]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Consensus pattern: [LIVMF]-x(2)-[HDY]-[EQ]-[FYW]-x-[KR]-H-G-x-C
- [H is an active site residue]
- [C is involved in a disulfide bond]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: genome polyproteins from Bovine
- viral diarrhea virus and Hog cholera virus. It seems that these pestiviruses
- polyproteins include a RNAse T2-like domain [8].
-
- -Last update: October 1993 / Patterns and text revised.
-
- [ 1] Watanabe H., Naitoh A., Suyama Y., Inokuchi N., Shimada H., Koyama T.,
- Ohgi K., Irie M.
- J. Biochem. 108:303-310(1990).
- [ 2] Haring V., Gray J.E., McClure B.A., Anderson M.A., Clarke A.E.
- Science 250:937-941(1990).
- [ 3] McClure B.A., Haring V., Ebert P.R., Anderson M.A., Simpson R.J.,
- Sakiyama F., Clarke A.E.
- Nature 342:95957(1989).
- [ 4] Loeffler A., Glund K., Irie M.
- Eur. J. Biochem. 214:627-633(1993).
- [ 5] Meador J. III, Kennell D.
- Gene 95:1-7(1990).
- [ 6] Kawata Y., Sakiyama F., Hayashi F., Kyogoku Y.
- Eur. J. Biochem. 187:255-262(1990).
- [ 7] Kurihara H., Mitsui Y., Ohgi K., Irie M., Mizuno H., Nakamura K.T.
- FEBS Lett. 306:189-192(1992).
- [ 8] Bairoch A.
- Unpublished observations (1993).
-