HMFB_METFE
ID HMFB_METFE Reviewed; 69 AA.
AC P19267;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=DNA-binding protein HMf-2 {ECO:0000303|PubMed:2377617};
DE AltName: Full=Archaeal histone B;
GN Name=hmfB {ECO:0000303|PubMed:7809089};
OS Methanothermus fervidus.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanothermaceae; Methanothermus.
OX NCBI_TaxID=2180;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-50, FUNCTION,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=2377617; DOI=10.1073/pnas.87.15.5788;
RA Sandman K.M., Krzycki J.A., Dobrinski B., Lurz R., Reeve J.N.;
RT "HMf, a DNA-binding protein isolated from the hyperthermophilic archaeon
RT Methanothermus fervidus, is most closely related to histones.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:5788-5791(1990).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND INDUCTION.
RX PubMed=7809089; DOI=10.1073/pnas.91.26.12624;
RA Sandman K.M., Grayling R.A., Dobrinski B., Lurz R., Reeve J.N.;
RT "Growth-phase-dependent synthesis of histones in the archaeon
RT Methanothermus fervidus.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:12624-12628(1994).
RN [3]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF ARG-10; LYS-13; ARG-19; VAL-20;
RP ARG-52; LYS-53; THR-54 AND LYS-56.
RX PubMed=10704305; DOI=10.1006/jmbi.2000.3546;
RA Soares D.J., Sandman K., Reeve J.N.;
RT "Mutational analysis of archaeal histone-DNA interactions.";
RL J. Mol. Biol. 297:39-47(2000).
RN [4]
RP CRYSTALLIZATION.
RX PubMed=8820495;
RX DOI=10.1002/(sici)1097-0134(199602)24:2<269::aid-prot16>3.0.co;2-l;
RA Decanniere K., Sandman K., Reeve J.N., Heinemann U.;
RT "Crystallization and preliminary X-ray characterization of the
RT Methanothermus fervidus histones HMfA and HMfB.";
RL Proteins 24:269-271(1996).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=8568866; DOI=10.1006/jmbi.1996.0016;
RA Starich M.R., Sandman K.M., Reeve J.N., Summers M.F.;
RT "NMR structure of HMfB from the hyperthermophile, Methanothermus fervidus,
RT confirms that this archaeal protein is a histone.";
RL J. Mol. Biol. 255:187-203(1996).
RN [6] {ECO:0007744|PDB:1A7W, ECO:0007744|PDB:1B6W}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS), AND SUBUNIT.
RX PubMed=11021968; DOI=10.1006/jmbi.2000.4104;
RA Decanniere K., Babu A.M., Sandman K., Reeve J.N., Heinemann U.;
RT "Crystal structures of recombinant histones HMfA and HMfB from the
RT hyperthermophilic archaeon Methanothermus fervidus.";
RL J. Mol. Biol. 303:35-47(2000).
RN [7] {ECO:0007744|PDB:5T5K}
RP X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) IN COMPLEX WITH DNA, SUBUNIT, AND
RP FUNCTION.
RX PubMed=28798133; DOI=10.1126/science.aaj1849;
RA Mattiroli F., Bhattacharyya S., Dyer P.N., White A.E., Sandman K.,
RA Burkhart B.W., Byrne K.R., Lee T., Ahn N.G., Santangelo T.J., Reeve J.N.,
RA Luger K.;
RT "Structure of histone-based chromatin in Archaea.";
RL Science 357:609-612(2017).
CC -!- FUNCTION: Binds and compacts DNA (95 to 150 base pairs) to form
CC nucleosome-like structures that contain positive DNA supercoils
CC (PubMed:2377617, PubMed:7809089, PubMed:10704305, PubMed:28798133).
CC Increases the resistance of DNA to thermal denaturation in vitro
CC (PubMed:2377617). {ECO:0000269|PubMed:10704305,
CC ECO:0000269|PubMed:2377617, ECO:0000269|PubMed:28798133,
CC ECO:0000269|PubMed:7809089}.
CC -!- SUBUNIT: Homodimer and heterodimer of HmfA and HmfB (PubMed:2377617,
CC PubMed:7809089, PubMed:10704305, PubMed:11021968, PubMed:28798133).
CC Heterodimers may be formed primarily when cells enter stationary growth
CC (PubMed:7809089). Dimers then assemble into higher oligomers, with the
CC DNA wrapped around the protein core (PubMed:28798133). Higher order
CC oligomerization of these structures can give rise to long, superhelical
CC fibers (in vitro) (PubMed:28798133). {ECO:0000269|PubMed:10704305,
CC ECO:0000269|PubMed:11021968, ECO:0000269|PubMed:2377617,
CC ECO:0000269|PubMed:28798133, ECO:0000269|PubMed:7809089}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:2377617}.
CC Chromosome {ECO:0000305|PubMed:2377617, ECO:0000305|PubMed:7809089}.
CC -!- INDUCTION: Expression is relatively low during exponential growth, and
CC is higher during the stationary phase. {ECO:0000269|PubMed:7809089}.
CC -!- SIMILARITY: Belongs to the archaeal histone HMF family. {ECO:0000305}.
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DR EMBL; M34778; AAA72080.1; -; Genomic_DNA.
DR PIR; A35959; A35959.
DR PDB; 1A7W; X-ray; 1.55 A; A=1-69.
DR PDB; 1B6W; X-ray; 2.05 A; A=1-69.
DR PDB; 1BFM; NMR; -; A/B=1-69.
DR PDB; 5T5K; X-ray; 4.00 A; A/B/C/D/E/F=1-69.
DR PDBsum; 1A7W; -.
DR PDBsum; 1B6W; -.
DR PDBsum; 1BFM; -.
DR PDBsum; 5T5K; -.
DR AlphaFoldDB; P19267; -.
DR SMR; P19267; -.
DR DIP; DIP-60390N; -.
DR OMA; CKHAGRK; -.
DR EvolutionaryTrace; P19267; -.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0006265; P:DNA topological change; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR003958; CBFA_NFYB_domain.
DR InterPro; IPR009072; Histone-fold.
DR Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Cytoplasm; Direct protein sequencing;
KW DNA-binding.
FT CHAIN 1..69
FT /note="DNA-binding protein HMf-2"
FT /id="PRO_0000154983"
FT REGION 19..21
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:28798133"
FT REGION 53..56
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:28798133"
FT SITE 13
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:28798133"
FT MUTAGEN 10
FT /note="R->S: Loss of formation of nucleosome-like
FT structures with DNA."
FT /evidence="ECO:0000269|PubMed:10704305"
FT MUTAGEN 13
FT /note="K->E,Q,T: Loss of formation of nucleosome-like
FT structures with DNA."
FT /evidence="ECO:0000269|PubMed:10704305"
FT MUTAGEN 19
FT /note="R->I,Q,S: Loss of formation of nucleosome-like
FT structures with DNA."
FT /evidence="ECO:0000269|PubMed:10704305"
FT MUTAGEN 20
FT /note="V->C: Loss of formation of nucleosome-like
FT structures with DNA."
FT /evidence="ECO:0000269|PubMed:10704305"
FT MUTAGEN 52
FT /note="R->K: No effect on formation of nucleosome-like
FT structures with DNA."
FT /evidence="ECO:0000269|PubMed:10704305"
FT MUTAGEN 53
FT /note="K->E,T: Loss of formation of nucleosome-like
FT structures with DNA."
FT /evidence="ECO:0000269|PubMed:10704305"
FT MUTAGEN 54
FT /note="T->A,C,K,R,S,V,Y: Loss of formation of nucleosome-
FT like structures with DNA."
FT /evidence="ECO:0000269|PubMed:10704305"
FT MUTAGEN 56
FT /note="K->E,T: Loss of formation of nucleosome-like
FT structures with DNA."
FT /evidence="ECO:0000269|PubMed:10704305"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:1A7W"
FT HELIX 22..49
FT /evidence="ECO:0007829|PDB:1A7W"
FT HELIX 57..65
FT /evidence="ECO:0007829|PDB:1A7W"
SQ SEQUENCE 69 AA; 7667 MW; F07D9DC1B6E5E3CF CRC64;
MELPIAPIGR IIKDAGAERV SDDARITLAK ILEEMGRDIA SEAIKLARHA GRKTIKAEDI
ELAVRRFKK
