Nucleotide and calcium‐induced conformational changes in histone H1

Tarkka, Tatu; Oikarinen, Jouko; Grundström, Thomas

doi:10.1016/s0014-5793(97)00238-x

Cited by 11 publications

(8 citation statements)

References 30 publications

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“…Hsp90 interacts with high affinity with all histones; in particular, Hsp90 binding to the C -terminal tail of histone Hl influences chromatin remodeling, which represents a fundamental event in the DSB repair pathways [ 167 ]. Indeed, Hsp90 interferes with the regulatory Ser-Pro-Lys-Lys motifs of histone H1 impairing phosphorylation and acetylation during stress or steroid action(s) [ 168 , 169 , 170 , 171 ].…”

Section: Role Of Hsp90 In the Genome Stability Maintenancementioning

confidence: 99%

Hsp90: A New Player in DNA Repair?

2015

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Heat shock protein 90 (Hsp90) is an evolutionary conserved molecular chaperone that, together with Hsp70 and co-chaperones makes up the Hsp90 chaperone machinery, stabilizing and activating more than 200 proteins, involved in protein homeostasis (i.e., proteostasis), transcriptional regulation, chromatin remodeling, and DNA repair. Cells respond to DNA damage by activating complex DNA damage response (DDR) pathways that include: (i) cell cycle arrest; (ii) transcriptional and post-translational activation of a subset of genes, including those associated with DNA repair; and (iii) triggering of programmed cell death. The efficacy of the DDR pathways is influenced by the nuclear levels of DNA repair proteins, which are regulated by balancing between protein synthesis and degradation as well as by nuclear import and export. The inability to respond properly to either DNA damage or to DNA repair leads to genetic instability, which in turn may enhance the rate of cancer development. Multiple components of the DNA double strand breaks repair machinery, including BRCA1, BRCA2, CHK1, DNA-PKcs, FANCA, and the MRE11/RAD50/NBN complex, have been described to be client proteins of Hsp90, which acts as a regulator of the diverse DDR pathways. Inhibition of Hsp90 actions leads to the altered localization and stabilization of DDR proteins after DNA damage and may represent a cell-specific and tumor-selective radiosensibilizer. Here, the role of Hsp90-dependent molecular mechanisms involved in cancer onset and in the maintenance of the genome integrity is discussed and highlighted.

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Section: Role Of Hsp90 In the Genome Stability Maintenancementioning

confidence: 99%

Hsp90: A New Player in DNA Repair?

2015

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“…This is indeed possible; an interaction of Ca 2+ with chromatin material has been reported in sympathetic neuronal cells [30]. It has also been shown in vitro that Ca 2+ and ATP induced structural changes on the histone H1, a major constituent of chromatin that contributes to chromatin condensation [31]. It is therefore possible that Ca 2+ -induced chromatin changes were allowing CaM or a CaM-binding protein to bind to chromatin.…”

Section: Discussionmentioning

confidence: 88%

Role of Ca2+ activation and bilobal structure of calmodulin in nuclear and nucleolar localization

Thorogate

Török

2007

Biochemical Journal

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Ca2+ signalling to the nucleus is thought to occur by calmodulin entry into the nucleus where calmodulin has many functions. In the present study we have investigated the role of Ca2+ and the N- and C-terminal lobes of calmodulin in its subnuclear targeting by using fluorescently labelled calmodulin and its mutants and confocal microscopy. Our data show, first, that Ca2+ stimulation induces a reorganization of subnuclear structures to which apo-calmodulin can bind. Secondly, Ca2+-independent association of the C-terminal lobe is seen with subnuclear structures such as chromatin, the nuclear envelope and the nucleoli. Thirdly, Ca2+-dependent accumulation of both calmodulin and the C-terminal calmodulin lobe occurs in the nucleoli. The N-terminal lobe of calmodulin does not show significant binding to subnuclear structures although, similarly to the C-terminal lobe, it accumulates in the nucleoplasm of wheat germ agglutinin-blocked nuclei suggesting that a facilitated nuclear export mechanism exists for calmodulin.

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“…3 suggest that these mutants have catalytic activities which depend on the stability of the conformation around the putative active sites. Therefore, these mutants may have active sites with local structures which are not substantial enough to be detected by macroscopic analysis, such as CD measurement, or the proper conformations around active sites may be generated only when the substrate binds to them, namely an induced folding mechanism [23–25].…”

Section: Resultsmentioning

confidence: 99%

Permutation of modules or secondary structure units creates proteins with basal enzymatic properties

Kobayashi

Yanagawa

1999

FEBS Letters

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The RNase activity of barnase mutants obtained by the permutation of modules or secondary structure units was investigated. Four of the 45 mutants had weak but distinct RNase activity, and they had unique optimum pHs and temperatures like natural enzymes. One of the active mutants had an ordered conformation, but the others did not. An active mutant having disordered conformation formed an ordered conformation in the presence of GMP, which is an inhibitor of this mutant. These results indicate that the amino acid sequences derived from barnase have sufficient plasticity to be rearranged into different proteins with basal enzymatic properties.z 1999 Federation of European Biochemical Societies.

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Nucleotide and calcium‐induced conformational changes in histone H1

Cited by 11 publications

References 30 publications

Hsp90: A New Player in DNA Repair?

Hsp90: A New Player in DNA Repair?

Role of Ca2+ activation and bilobal structure of calmodulin in nuclear and nucleolar localization

Permutation of modules or secondary structure units creates proteins with basal enzymatic properties

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