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Histone chaperones and nucleosome assembly.
Akey CW, Luger K. Akey CW, et al. Curr Opin Struct Biol. 2003 Feb;13(1):6-14. doi: 10.1016/s0959-440x(03)00002-2. Curr Opin Struct Biol. 2003. PMID: 12581654 Review.
The nucleosome and its protein core, the histone octamer, have twofold symmetry, which histone chaperones may use to bind core histones. Recent studies suggest that the nucleoplasmin pentamer may mediate histone storage, sperm chromatin decondensation and nucleosome assemb …
The nucleosome and its protein core, the histone octamer, have twofold symmetry, which histone chaperones may use to bind core histones. Rec …
Crystal structure and function of human nucleoplasmin (npm2): a histone chaperone in oocytes and embryos.
Platonova O, Akey IV, Head JF, Akey CW. Platonova O, et al. Among authors: akey cw. Biochemistry. 2011 Sep 20;50(37):8078-89. doi: 10.1021/bi2006652. Epub 2011 Aug 24. Biochemistry. 2011. PMID: 21863821 Free PMC article.
Fluorescence resonance energy transfer experiments and biochemical analysis of loop mutations support the premise that nucleoplasmins form decamers when they bind H2A-H2B dimers and H3-H4 tetramers simultaneously. ...When taken together, our data provide insights into the …
Fluorescence resonance energy transfer experiments and biochemical analysis of loop mutations support the premise that nucleoplasmins …
Visualization of transport-related configurations of the nuclear pore transporter.
Akey CW. Akey CW. Biophys J. 1990 Aug;58(2):341-55. doi: 10.1016/S0006-3495(90)82381-X. Biophys J. 1990. PMID: 2207242 Free PMC article.
This data confirms previous observations on NPC transporters labeled with nucleoplasmin-gold (Akey, C.W., and D.S. Goldfarb. 1989. J. Cell Biol. 109:971-982) and allows a working model of the central NPC transporter to be proposed. ...
This data confirms previous observations on NPC transporters labeled with nucleoplasmin-gold (Akey, C.W., and D.S. Goldfarb. 1989. J. …
The crystal structure of nucleoplasmin-core: implications for histone binding and nucleosome assembly.
Dutta S, Akey IV, Dingwall C, Hartman KL, Laue T, Nolte RT, Head JF, Akey CW. Dutta S, et al. Among authors: akey cw. Mol Cell. 2001 Oct;8(4):841-53. doi: 10.1016/s1097-2765(01)00354-9. Mol Cell. 2001. PMID: 11684019 Free article.
Currently, there is a paucity of data on their mechanism of action. We now present the structure of an N-terminal domain of nucleoplasmin (Np-core) at 2.3 A resolution. The Np-core monomer is an eight-stranded beta barrel that fits snugly within a stable pentamer. ...
Currently, there is a paucity of data on their mechanism of action. We now present the structure of an N-terminal domain of nucleoplasmin …
The structure and function of Xenopus NO38-core, a histone chaperone in the nucleolus.
Namboodiri VM, Akey IV, Schmidt-Zachmann MS, Head JF, Akey CW. Namboodiri VM, et al. Among authors: akey cw. Structure. 2004 Dec;12(12):2149-60. doi: 10.1016/j.str.2004.09.017. Structure. 2004. PMID: 15576029 Free article.
Xenopus NO38 is an abundant nucleolar chaperone and a member of the nucleoplasmin (Np) family. Here, we report high-resolution crystal structures of the N-terminal domain of NO38, as a pentamer and a decamer. ...
Xenopus NO38 is an abundant nucleolar chaperone and a member of the nucleoplasmin (Np) family. Here, we report high-resolution crysta …
Protein import through the nuclear pore complex is a multistep process.
Akey CW, Goldfarb DS. Akey CW, et al. J Cell Biol. 1989 Sep;109(3):971-82. doi: 10.1083/jcb.109.3.971. J Cell Biol. 1989. PMID: 2475512 Free PMC article.
The probes used in these experiments were (a) mAb-414, which cross-reacts with Xenopus nucleoporins containing O-linked N-acetyl glucosamines; (b) wheat germ agglutinin, a transport inhibitor; and (c) nucleoplasmin, a transport substrate. Strong binding sites of the three …
The probes used in these experiments were (a) mAb-414, which cross-reacts with Xenopus nucleoporins containing O-linked N-acetyl glucosamine …
The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding.
Namboodiri VM, Dutta S, Akey IV, Head JF, Akey CW. Namboodiri VM, et al. Among authors: akey cw. Structure. 2003 Feb;11(2):175-86. doi: 10.1016/s0969-2126(03)00007-8. Structure. 2003. PMID: 12575937 Free article.
The nucleoplasmin-like protein from Drosophila (dNLP) functions as a chaperone for core histones and may remodel chromatin in embryos. ...The monomer has an eight-stranded, beta barrel topology that is similar to nucleoplasmin (Np). However, a signature beta hairpin …
The nucleoplasmin-like protein from Drosophila (dNLP) functions as a chaperone for core histones and may remodel chromatin in embryos …
Purification, crystallization and preliminary X-ray analysis of the N-terminal domain of NO38, a nucleolar protein from Xenopus laevis.
Namboodiri VM, Schmidt-Zachmann MS, Head JF, Akey CW. Namboodiri VM, et al. Among authors: akey cw. Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 2):2325-7. doi: 10.1107/S0907444904023959. Epub 2004 Nov 26. Acta Crystallogr D Biol Crystallogr. 2004. PMID: 15583381
NO38 is a multidomain protein that belongs to the nucleoplasmin (Np) family. Previous studies have suggested that acidic chaperones such as Np may function as histone-storage platforms. ...
NO38 is a multidomain protein that belongs to the nucleoplasmin (Np) family. Previous studies have suggested that acidic chaperones s …