Entry
Name
ribonuclease E;
endoribonuclease E;
RNase E;
Rne protein
Class
Hydrolases;
Acting on ester bonds;
Endoribonucleases producing 5'-phosphomonoesters
BRITE hierarchy
Reaction(IUBMB)
Endonucleolytic cleavage of single-stranded RNA in A- and U-rich regions
Comment
RNase E is a bacterial ribonuclease that plays a role in the processing of ribosomal RNA (9S to 5S rRNA), the chemical degradation of bulk cellular RNA, the decay of specific regulatory, messenger and structural RNAs and the control of plasmid DNA replication [1]. The enzyme binds to monophosphorylated 5' ends of substrates but exhibits sequential cleavages in the 3' to 5' direction [1]. 2'-O-Methyl nucleotide substitutions at RNase E binding sites do not prevent binding but do prevent cleavage of non-modified target sequences 5' to that locus [1]. In Escherichia coli, the enzyme is found in the RNA degradosome. The C-terminal half of the protein contains binding sites for the three other major degradosomal components, the DEAD-box RNA helicase Rh1B, enolase (EC
4.1.1.11 ) and polynucleotide phosphorylase (EC
2.7.7.8 ).
History
EC 3.1.26.12 created 2008
Orthology
Genes
ECOO : ECRM13514_1375(rne)
ECOH : ECRM13516_1332(rne)
ELR : ECO55CA74_06555(rne)
EDJ : ECDH1ME8569_1019(rne)
SETC : CFSAN001921_11250(rne)
SEEN : SE451236_11775(rne)
SENH : CFSAN002069_03095(rne)
SEEH : SEEH1578_15155(rne)
SENJ : CFSAN001992_05715(rne)
SEEC : CFSAN002050_12315(rne)
SEEB : SEEB0189_013645(rne)
SENC : SEET0819_12570(rne)
REE : electrica_03172(rne)
RTG : NCTC13098_04465(rne)
CLAP : NCTC11466_02822(rne)
KIE : NCTC12125_01813(rne_1)
AHN : NCTC12129_03131(rne)
METY : MRY16398_21220(rne)
PSHI : SAMEA2665130_1855(rne)
YPI : YpsIP31758_1569(rne)
SERS : SERRSCBI_08925(rne)
SFJ : SAMEA4384070_1931(rne)
SOF : NCTC11214_04925(rne)
EHD : ERCIPSTX3056_131(rne)
BAPF : BUMPF009_CDS00249(rne)
BAPG : BUMPG002_CDS00250(rne)
BAPU : BUMPUSDA_CDS00249(rne)
BAPW : BUMPW106_CDS00249(rne)
TPTY : NCTC11468_01493(rne_1)
PHEI : NCTC12003_01655(rne)
LRI : NCTC12151_01931(rne)
HIC : NTHIC486_00573(rng_1)
HPIT : NCTC13334_01983(rne)
HHZ : NCTC10839_00919(rng_1)
HAEG : NCTC8502_00728(rne)
ADP : NCTC12871_01064(rne)
ALIG : NCTC10568_01781(rne)
ASEG : NCTC10977_01927(rne)
PAET : NCTC13378_00212(rne)
XPH : XppCFBP6546_02105(XppCFBP6546P_02105)
VCO : VC0395_A1615 VC0395_A1616(rne)
VAU : VANGNB10_cI1842(rne)
VPL : SA104470976_00784(rne)
PPRC : PFLCHA0_c18240(rne)
PMUD : NCTC8068_01450(rne)
PFW : PF1751_v1c42220(rne)
PTAE : NCTC10697_01229(rne)
MCUN : NCTC10297_00212(rne)
LJR : NCTC11533_00658(rne)
LCJ : NCTC11976_01331(rne)
LWA : SAMEA4504053_2531(rne)
LSS : NCTC12082_02813(rne)
LADL : NCTC12735_00336(rne)
LANT : TUM19329_09340(rne)
GAI : IMCC3135_11725(rng_1)
HAXI : HAALTHF_32940n HAALTHF_32950n
AEL : NCTC12917_02095(rne)
CHJ : NCTC10426_01406(rne)
NMQ : NMBM04240196_0204(rne)
NWE : SAMEA3174300_0008(rne)
NZO : SAMEA4504057_2130(rne)
NCI : NCTC10296_00124(rne)
NCZ : NCTC10294_01715(rne)
NANI : NCTC12227_00119(rne)
NMB : MON40_09595 MON40_13140
ECOR : SAMEA4412678_1414(rng_2)
BPM : BURPS1710b_2918(rne)
BPL : BURPS1106A_2863(rne)
BCJ : BCAL0982(rne2) BCAL2888(rne1)
PLG : NCTC10937_01699(rne)
LMIR : NCTC12852_01985(rne)
BUO : BRPE64_ACDS19910(rne)
BTRM : SAMEA390648702554(ams)
AXX : ERS451415_01439(rne)
MBAC : BN1209_0920 BN1209_0921
URU : DSM104443_02209(rne)
UPL : DSM104440_02038(rne)
RBS : RHODOSMS8_00749(rne)
BSW : IY71_04550 IY71_12520
BSG : IY72_04280 IY72_12060
BHS : BM1374165_00956(rne)
BTX : BM1374166_01128(rne)
BEZ : NCTC12898_00747(rne)
MAQU : Maq22A_c14930(cafA)
MTUN : MTUNDRAET4_1174(rne)
TSV : DSM104635_01652(rne_1) DSM104635_02264(rne_2)
SIT : TM1040_1459 TM1040_1967
PHP : PhaeoP97_01343(rne) PhaeoP97_02251
PPIC : PhaeoP14_01266(rne) PhaeoP14_02166
PHQ : D1820_02855 D1820_06795
LMD : METH_05535 METH_10485
YPAC : CEW88_03540 CEW88_08130
TPRO : Ga0080559_TMP2938 Ga0080559_TMP3537
PABY : Ga0080574_TMP1311 Ga0080574_TMP4049
SINL : DSM14862_01580(rne)
SPSE : SULPSESMR1_01418(rne)
RMM : ROSMUCSMR3_00060(rne)
LALG : LentiSH36_01104(rne)
LVS : LOKVESSMR4R_01334(rne)
CBOT : ATE48_01700 ATE48_18225
SFLA : SPHFLASMR4Y_00541(rne)
ASV : WG31_10350 WG31_10375
APOM : CPF11_10255 CPF11_10280
ACET : DS739_10115 DS739_10140
EBLA : JGUZn3_23450(rne_2)
HTQ : FRZ44_14690(rne) FRZ44_38500
HADH : FRZ61_14420(rne) FRZ61_36870
MBAI : MB901379_03351(rng)
MKY : IWGMT90018_20380(rne)
MPHL : MPHLCCUG_03595(rng)
MAUU : NCTC10437_03726(rng)
MALV : MALV_00180 MALV_00190 MALV_54950
MFLV : NCTC10271_01703(rng)
MSAL : DSM43276_01468(rng)
CDIP : ERS451417_01798(rne)
CUJ : CUL131002_1686c(rne)
CMIN : NCTC10288_00571(rne)
CCYS : SAMEA4530656_0438(rne)
NFR : ERS450000_02755(rng)
NAD : NCTC11293_02337(rng)
RCR : NCTC10994_01039(rng)
SLE : sle_46370(sle_46370)
SXT : KPP03845_102765(rne)
AMAU : DSM26151_15580(rne)
PSEV : USB125703_00061(rne)
AAGI : NCTC2676_1_01151(rng)
DCO : SAMEA4475696_1145(rng)
PAUS : NCTC13651_01544(rng)
NAQU : ENKNEFLB_03357(rng)
TBW : NCTC13354_01776(rng)
AHW : NCTC11636_00116(rng)
AIR : NCTC12972_01099(rng)
AVC : NCTC10951_00426(rne)
SYR : SynRCC307_2177(cafA)
SYX : SynWH7803_0372(cafA)
TVN : NIES2134_108600(rne)
LET : O77CONTIG1_02770(rne)
CHON : NIES4102_37020(rne)
SYP : SYNPCC7002_A0788(rne)
SYNN : NIES970_08300(rne_1) NIES970_08480(rne_2)
NSPH : BDGGKGIB_02169(rng)
ROL : CA51_14170(rne) CA51_21530
AHEL : Q31a_23930(rne) Q31a_53820
LCRE : Pla8534_26970(rne) Pla8534_50900
LPAV : PLANPX_2344 PLANPX_5867
PND : Pla175_06200(rng) Pla175_33560
» show all
Taxonomy
Reference
Authors
Feng Y, Vickers TA, Cohen SN.
Title
The catalytic domain of RNase E shows inherent 3' to 5' directionality in cleavage site selection.
Journal
Reference
Authors
Ehretsmann CP, Carpousis AJ, Krisch HM.
Title
Specificity of Escherichia coli endoribonuclease RNase E: in vivo and in vitro analysis of mutants in a bacteriophage T4 mRNA processing site.
Journal
Reference
Authors
Cormack RS, Genereaux JL, Mackie GA.
Title
RNase E activity is conferred by a single polypeptide: overexpression, purification, and properties of the ams/rne/hmp1 gene product.
Journal
Sequence
Reference
Authors
Vanzo NF, Li YS, Py B, Blum E, Higgins CF, Raynal LC, Krisch HM, Carpousis AJ.
Title
Ribonuclease E organizes the protein interactions in the Escherichia coli RNA degradosome.
Journal
Sequence
Reference
Authors
Steege DA.
Title
Emerging features of mRNA decay in bacteria.
Journal
Reference
Authors
Callaghan AJ, Grossmann JG, Redko YU, Ilag LL, Moncrieffe MC, Symmons MF, Robinson CV, McDowall KJ, Luisi BF.
Title
Quaternary structure and catalytic activity of the Escherichia coli ribonuclease E amino-terminal catalytic domain.
Journal
Other DBs
ExPASy - ENZYME nomenclature database: 3.1.26.12