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Ribonuclease T2-like

 
Known also as: RNase T2-like

Known abbreviations: Rny1p, YPL123C


FUNCTION:
  • Regulation of membrane permeability or stability during stress conditions (secreting an RNase to degrade membrane-bound RNAs) (PMID: 11158587, 14586131),
  • perhabs involved in maintaining cellular homeostasis (PMID: 11158587),
  • involved in cell growth at high salt concentrations or at high temperatures (PMID: 11158587),
  • involved in formation of normal vacuolar morphology, cell size and shape (PMID: 11158587).

REACTION:

Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates (EntrezEnz)

CELLULAR LOCALIZATION:
  • extracellular (PMID: 11158587)
  • in compartments of the endomembrane system (PMID: 11158587)



Activities in which Ribonuclease T2-like is involved: Pathways in which Ribonuclease T2-like is involved:

NCBI GI number(s): 574961
74676326
Species: Saccharomyces cerevisiae

Links to other databases:

Database ID Link
Uniprot Q02933 Q02933
BRENDA - -
KEGG sce:YPL123C sce:YPL123C
PFAM: PF00445
PF00445
InterPro: IPR001568
IPR018188
IPR001568
IPR018188
CATH: - -
SCOP: - -


Protein sequence:
MLLKNLHSLLQLPIFSNGADKGIEPNCPINIPLSCSNKTDIDNSCCFEYP
GGIFLQTQFWNYFPSKNDLNETELVKELGPLDSFTIHGLWPDNCHGGYQQ
FCNRSLQIDDVYYLLHDKKFNNNDTSLQISGEKLLEYLDLYWKSNNGNHE
SLWIHEFNKHGTCISTIRPECYTEWGANSVDRKRAVYDYFRITYNLFKKL
DTFSTLEKNNIVPSVDNSYSLEQIEAALSKEFEGKKVFIGCDRHNSLNEV
WYYNHLKGSLLSEMFVPMDSLAIRTNCKKDGIKFFPKGYVPTFRRRPNKG
ARYRGVVRLSNINNGDQMQGFLIKNGHWMSQGTPANYELIKSPYGNYYLR
TNQGFCDIISSSSNELVCKFRNIKDAGQFDFDPTKGGDGYIGYSGNYNWG
GDTYPRRRNQSPIFSVDDEQNSKKYKFKLKFIKN

Ribonuclease T2-like (Saccharomyces cerevisiae) is product of expression of RNT1 gene.

Ribonuclease T2-like (Saccharomyces cerevisiae) belongs to following protein families:
References:

Title Authors Journal Publication date (Issue) PubMed ID
Relaxed transcription in Arabidopsis mitochondria is counterbalanced by RNA stability control mediated by polyadenylation and polynucleotide phosphorylase. Holec S, Lange H, Kuhn K, Alioua M, Borner T, Gagliardi D Mol Cell Biol 2006-04-01 (26) 16537927
PNPase activity determines the efficiency of mRNA 3'-end processing, the degradation of tRNA and the extent of polyadenylation in chloroplasts. Walter M, Kilian J, Kudla J EMBO J 2002-12-16 (21) 12486011
Characterization of Rny1, the Saccharomyces cerevisiae member of the T2 RNase family of RNases: unexpected functions for ancient enzymes? MacIntosh GC, Bariola PA, Newbigin E, Green PJ Proc Natl Acad Sci U S A 2001-02-01 (98) 11158587
The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI. Bussey H, Storms RK, Ahmed A, Albermann K, Allen E, Ansorge W, Araujo R, Aparicio A, Barrell B, Badcock K, Benes V, Botstein D, Bowman S, Bruckner M, Carpenter J, Cherry JM, Chung E, Churcher C, Coster F, Davis K, Davis RW, Dietrich FS, Delius H, DiPaolo T, Hani J, et al. Nature 1997-05-01 (387) 9169875
Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae. Hu Y, Rolfs A, Bhullar B, Murthy TV, Zhu C, Berger MF, Camargo AA, Kelley F, McCarron S, Jepson D, Richardson A, Raphael J, Moreira D, Taycher E, Zuo D, Mohr S, Kane MF, Williamson J, Simpson A, Bulyk ML, Harlow E, Marsischky G, Kolodner RD, LaBaer J Genome Res 2007-04-01 (17) 17322287
Global analysis of protein expression in yeast. Ghaemmaghami S, Huh WK, Bower K, Howson RW, Belle A, Dephoure N, O'Shea EK, Weissman JS Nature 2003-10-16 (425) 14562106
The RNase Rny1p cleaves tRNAs and promotes cell death during oxidative stress in Saccharomyces cerevisiae. Thompson DM, Parker R J Cell Biol 2009-04-06 (185) 19332891



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Last modification of this entry: 2011-01-22 13:15:35
Edited by a user: kasia
Edited content: Changed abbreviations.

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