NDLI: Archaeal chromatin proteins histone HMtB and Alba have lost DNA-binding ability in laboratory strains of Methanothermobacter thermautotrophicus

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Archaeal chromatin proteins histone HMtB and Alba have lost DNA-binding ability in laboratory strains of Methanothermobacter thermautotrophicus

Content Provider	Springer Nature Link
Author	Sandman, Kathleen Louvel, Hélène Samson, Rachel Y. Pereira, Suzette L. Reeve, John N.
Copyright Year	2008
Abstract	Alignments of the sequences of the all members of the archaeal histone and Alba1 families of chromatin proteins identified isoleucine residues, I19 in HMtB and I39 in MtAlba, in Methanothermobacter thermautotrophicus, at locations predicted to be directly involved in DNA binding. In all other HMfB family members, residue 19 is an arginine (R19), and either arginine or lysine is present in almost all other Alba1 family members at the structural site equivalent to I39 in MtAlba. Electrophoretic mobility shift assays revealed that recombinant HMtB and MtAlba do not bind DNA, but variants constructed with R19 and R39, respectively, bound DNA; and whereas MtAlba(I19) did not bind RNA, MtAlba(R19) bound both single stranded RNA and tRNA. Amplification and sequencing of MT0254 (encodes HMtB) and MT1483 (encodes MtAlba) from several Methanothermobacter thermautotrophicus lineages has revealed that HMtB and MtAlba had arginine residues at positions 19 and 39, respectively, in the original isolate and that spontaneous mutations must have occurred, and been fixed, in some laboratory lineages that now have HMtB(I19) and MtAlba(I39). The retention of these variants suggests some continuing functions and fusion of the HMtB(I19) sequence to HMtA2 resulted in a protein that folds to form a histone fold heterodimer that binds and compacts DNA. The loss of DNA binding by HMtB(I19) does not therefore prevent HMtB from participating in DNA interactions as one partner of an archaeal histone heterodimer.
Starting Page	811
Ending Page	817
Page Count	7
File Format	PDF
ISSN	14310651
Journal	Extremophiles
Volume Number	12
Issue Number	6
e-ISSN	14334909
Language	English
Publisher	Springer Japan
Publisher Date	2008-08-23
Publisher Place	Japan
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Archaea Chromatin proteins Spontaneous mutations Nucleic acid binding Ecology Biotechnology Microbiology
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Medicine Microbiology

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