CRHR_SYNY3
ID CRHR_SYNY3 Reviewed; 492 AA.
AC Q55804;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=RNA helicase CrhR {ECO:0000303|PubMed:11027719};
DE EC=3.6.4.13 {ECO:0000269|PubMed:15542859};
GN Name=crhR {ECO:0000303|PubMed:11027719};
GN Synonyms=deaD {ECO:0000303|PubMed:8905231}; OrderedLocusNames=slr0083;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP INDUCTION UNDER REDOX CONTROL.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=11027719; DOI=10.1104/pp.124.2.703;
RA Kujat S.L., Owttrim G.W.;
RT "Redox-regulated RNA helicase expression.";
RL Plant Physiol. 124:703-714(2000).
RN [3]
RP FUNCTION, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, AND ACTIVITY
RP REGULATION.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=15542859; DOI=10.1074/jbc.m409700200;
RA Chamot D., Colvin K.R., Kujat-Choy S.L., Owttrim G.W.;
RT "RNA structural rearrangement via unwinding and annealing by the
RT cyanobacterial RNA helicase, CrhR.";
RL J. Biol. Chem. 280:2036-2044(2005).
RN [4]
RP INDUCTION BY COLD SHOCK.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=16840531; DOI=10.1093/nar/gkl426;
RA Patterson-Fortin L.M., Colvin K.R., Owttrim G.W.;
RT "A LexA-related protein regulates redox-sensitive expression of the
RT cyanobacterial RNA helicase, crhR.";
RL Nucleic Acids Res. 34:3446-3454(2006).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY COLD SHOCK, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=19926653; DOI=10.1099/mic.0.031823-0;
RA Prakash J.S., Krishna P.S., Sirisha K., Kanesaki Y., Suzuki I., Shivaji S.,
RA Murata N.;
RT "An RNA helicase, CrhR, regulates the low-temperature-inducible expression
RT of heat-shock genes groES, groEL1 and groEL2 in Synechocystis sp. PCC
RT 6803.";
RL Microbiology 156:442-451(2010).
RN [6]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=22368073; DOI=10.1093/pcp/pcs020;
RA Rosana A.R., Ventakesh M., Chamot D., Patterson-Fortin L.M., Tarassova O.,
RA Espie G.S., Owttrim G.W.;
RT "Inactivation of a low temperature-induced RNA helicase in Synechocystis
RT sp. PCC 6803: physiological and morphological consequences.";
RL Plant Cell Physiol. 53:646-658(2012).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=22575444; DOI=10.1016/j.bbabio.2012.04.016;
RA Sireesha K., Radharani B., Krishna P.S., Sreedhar N., Subramanyam R.,
RA Mohanty P., Prakash J.S.;
RT "RNA helicase, CrhR is indispensable for the energy redistribution and the
RT regulation of photosystem stoichiometry at low temperature in Synechocystis
RT sp. PCC6803.";
RL Biochim. Biophys. Acta 1817:1525-1536(2012).
RN [8]
RP POSSIBLE FUNCTION IN AUTOREGULATION, SUBCELLULAR LOCATION, INDUCTION BY
RP COLD, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=23119089; DOI=10.1371/journal.pone.0048683;
RA Rosana A.R., Chamot D., Owttrim G.W.;
RT "Autoregulation of RNA helicase expression in response to temperature
RT stress in Synechocystis sp. PCC 6803.";
RL PLoS ONE 7:E48683-E48683(2012).
RN [9]
RP ACTIVITY REGULATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=24509313; DOI=10.1128/jb.01362-13;
RA Tarassova O.S., Chamot D., Owttrim G.W.;
RT "Conditional, temperature-induced proteolytic regulation of cyanobacterial
RT RNA helicase expression.";
RL J. Bacteriol. 196:1560-1568(2014).
RN [10]
RP SUBCELLULAR LOCATION.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=27215789; DOI=10.1128/jb.00267-16;
RA Rosana A.R., Whitford D.S., Fahlman R.P., Owttrim G.W.;
RT "Cyanobacterial RNA Helicase CrhR Localizes to the Thylakoid Membrane
RT Region and Cosediments with Degradosome and Polysome Complexes in
RT Synechocystis sp. Strain PCC 6803.";
RL J. Bacteriol. 198:2089-2099(2016).
RN [11]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=32209657; DOI=10.1074/jbc.ra120.013148;
RA Rosana A.R.R., Whitford D.S., Migur A., Steglich C., Kujat-Choy S.L.,
RA Hess W.R., Owttrim G.W.;
RT "RNA helicase-regulated processing of the Synechocystis rimO-crhR operon
RT results in differential cistron expression and accumulation of two sRNAs.";
RL J. Biol. Chem. 295:6372-6386(2020).
CC -!- FUNCTION: An ATP-dependent bidirectional RNA helicase with RNA-
CC dependent ATPase activity; does not unwind dsDNA, uses only (d)ATP
CC (PubMed:15542859). Also has ATP-dependent RNA annealing activity;
CC concurrent annealing and helicase activity promote strand-exchange
CC activity (PubMed:15542859). In vitro has low helicase processivity,
CC annealing processivity is probably higher (PubMed:15542859). Required
CC for correct cold adaptation, probably by aiding translation of mRNAs
CC required for photosynthesis and electron transport (PubMed:22575444).
CC Probably regulates the cold-shock-inducible expression of the GroESL
CC chaperones (PubMed:19926653). May partially regulate its own expression
CC at both the transcriptional and post-transcriptional level (experiments
CC used a construct expressing a 25 kDa trunacted protein which might have
CC dominant-negative effects); is probably not directly involved in the
CC pathway responsible for mRNA degradation (PubMed:23119089).
CC {ECO:0000269|PubMed:15542859, ECO:0000269|PubMed:19926653,
CC ECO:0000269|PubMed:22575444, ECO:0000305|PubMed:23119089}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000269|PubMed:15542859};
CC -!- ACTIVITY REGULATION: Helicase inhibited by the slowly-hydrolyzing ATP
CC analog ATP-gamma-S (PubMed:15542859). Protein is rapidly degraded upon
CC shifting from 20 to 30 degrees Celsius, the degradation machinery is
CC only transiently present in cells grown at 30 degrees Celsius, is
CC inhibited by commercial protease inhibitors and requires full-length
CC protein expression (the N-terminal fragment does not induce proteolysis
CC although it can be degraded by wild-type extract) (PubMed:24509313).
CC {ECO:0000269|PubMed:15542859, ECO:0000269|PubMed:24509313}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19926653,
CC ECO:0000269|PubMed:22368073, ECO:0000269|PubMed:23119089,
CC ECO:0000269|PubMed:27215789}. Cell inner membrane
CC {ECO:0000305|PubMed:27215789}; Peripheral membrane protein
CC {ECO:0000305}. Cellular thylakoid membrane
CC {ECO:0000269|PubMed:27215789}; Peripheral membrane protein
CC {ECO:0000305}. Note=A small amount is localized to the cell inner
CC membrane and the thylakoid membrane, and cosediments with polysomes.
CC {ECO:0000269|PubMed:27215789}.
CC -!- INDUCTION: Constitutively expressed; higher levels are found in light-
CC grown cells and lower levels in dark cells unless grown in glucose (at
CC protein level) (PubMed:11027719, PubMed:23119089). Transcript level is
CC regulated by the redox state of the plastoquinone pool; transcript
CC accumulates when electrons flow between PSII and cytochrome b6-f
CC complex (reduction of the electron transport chain) (PubMed:11027719).
CC LexA-like repressor probably represses its expression at least in part
CC (PubMed:16840531). Induced by cold with maximal RNA induction at 15
CC degrees Celsius and maximal protein induction at 15-20 degrees Celsius
CC (at protein level) (PubMed:23119089). Also expressed as part of the
CC rimO-chrR operon; expression is greater at 20 than 30 degrees Celsius.
CC The rimO-crhR transcript is processed between the 2 genes by RNase E
CC (rne) (PubMed:32209657). {ECO:0000269|PubMed:11027719,
CC ECO:0000269|PubMed:16840531, ECO:0000269|PubMed:23119089,
CC ECO:0000269|PubMed:32209657}.
CC -!- DISRUPTION PHENOTYPE: Probably a complete knockout; no growth phenotype
CC or large transcript changes at 34 degrees Celsius; at 24 degrees
CC Celsius growth is considerably slower, while expression of a few genes
CC is decreased (groES, groEL1, groEL2 and sll1611) or increased (pyrB,
CC sll1911, sll1515 and rimO) (at 70 umol/photon/m(2)/s, 1% CO(2))
CC (PubMed:19926653, PubMed:32209657). At 24 degrees reduced chlorophyll
CC and phycocyanin content and a gradual reduction in photosynthetic O(2)
CC evolution; cells are locked in state 1 and unable to undergo state
CC transitions, the plastoquinone pool is oxidized, leading to down-
CC regulation of psaA and psaB transcripts and thus decreased PSI levels
CC (PubMed:22575444). A partial knockout allowing expression of the first
CC 224 residues as a 25 kDa truncated protein at 30 degrees Celsius has
CC reduced growth, 20% reduced O(2) evolution and 10% reduced electron
CC transport, at 20 degrees Celsius has similar, more severe effects; no
CC growth with rapid loss of viability, little to no photosynthetic O(2)
CC evolution, 50% reduced electron transport, decreased pigment content,
CC smaller cell size and considerable intracellular disorganization (at 30
CC umol/photon/m(2)/s, sterile air) (PubMed:22368073). The latter mutant
CC is able to concentrate inorganic carbon but cannot use it to fix CO(2)
CC (PubMed:22368073). The truncated protein is constitutively expressed at
CC 30 and 20 degrees Celsius and is no longer subject to normal regulation
CC i.e. has lost cold-shock induction and dark-induced repression
CC (PubMed:23119089, PubMed:24509313). {ECO:0000269|PubMed:19926653,
CC ECO:0000269|PubMed:22368073, ECO:0000269|PubMed:22575444,
CC ECO:0000269|PubMed:23119089, ECO:0000269|PubMed:24509313,
CC ECO:0000269|PubMed:32209657}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC {ECO:0000255|RuleBase:RU000492, ECO:0000305}.
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DR EMBL; BA000022; BAA10556.1; -; Genomic_DNA.
DR PIR; S76612; S76612.
DR AlphaFoldDB; Q55804; -.
DR SMR; Q55804; -.
DR DIP; DIP-48812N; -.
DR IntAct; Q55804; 4.
DR STRING; 1148.1001719; -.
DR PaxDb; Q55804; -.
DR EnsemblBacteria; BAA10556; BAA10556; BAA10556.
DR KEGG; syn:slr0083; -.
DR eggNOG; COG0513; Bacteria.
DR InParanoid; Q55804; -.
DR OMA; EHKDGQR; -.
DR PhylomeDB; Q55804; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034458; F:3'-5' RNA helicase activity; IDA:UniProtKB.
DR GO; GO:0032574; F:5'-3' RNA helicase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0033592; F:RNA strand annealing activity; IDA:UniProtKB.
DR GO; GO:0034057; F:RNA strand-exchange activity; IDA:UniProtKB.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Cytoplasm; Helicase;
KW Hydrolase; Membrane; Nucleotide-binding; Reference proteome;
KW Stress response; Thylakoid.
FT CHAIN 1..492
FT /note="RNA helicase CrhR"
FT /id="PRO_0000434785"
FT DOMAIN 38..207
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 234..379
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 451..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 7..35
FT /note="Q motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00552"
FT MOTIF 155..158
FT /note="DEAD box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 51..58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 492 AA; 55120 MW; 7D2801E515DB444B CRC64;
MTNTLTSTFA DLGLSEKRCQ LLADIGFEAP TQIQTEAIPL LLSGRDMLAQ SQTGTGKTAA
FALPLMDRID PEGDLQALIL TPTRELAQQV AEAMKDFSHE RRLFILNVYG GQSIERQIRS
LERGVQIVVG TPGRVIDLID RKKLKLETIQ WVVLDEADEM LSMGFIDDVK TILRKTPPTR
QTACFSATMP REIKELVNQF LNDPALVTVK QTQSTPTRIE QQLYHVPRGW SKAKALQPIL
EMEDPESAII FVRTKQTAAD LTSRLQEAGH SVDEYHGNLS QSQRERLVHR FRDGKIKLVV
ATDIAARGLD VNNLSHVVNF DLPDNAETYI HRIGRTGRAG KTGKAIALVE PIDRRLLRSI
ENRLKQQIEV CTIPNRSQVE AKRIEKLQEQ LKEALTGERM ASFLPLVREL SDEYDAQAIA
AAALQMIYDQ SCPHWMKSDW EVPEVDFNKP VLRRGRNAGG GQNKSGGGYQ GKPGKPRRSS
GGRRPAYSDR QQ
