Abstract:
:The hypothesis that distinct chromatin domains expand and are remodelled differently when they undergo transcription, replication or cell cycle processes is well accepted. The condensation changes by which chromosomes are transformed at the metaphase-interphase transition are especially interesting and therefore extensively studied by light microscopy; however, quantitative information of the size on specific small chromatin domains during the cell cycle is scarce. In this respect, a serious problem is the determination of structural features close to the resolution limit. In this report we use a novel approach to quantify the lateral extent of the 8q24/c-myc gene domain and the centromeric region of chromosome 8 in doubly labelled normal human foreskin fibroblasts using confocal laser scanning microscopy (CLSM). The domains were analysed in both metaphase spreads and interphase nuclei. These high precision measurements revealed a somewhat smaller (few 10s of nm) lateral extension of the centromere region in metaphase compared to interphase. Surprisingly, within the same cells the lateral extension of the 8q24/c-myc region was significantly smaller in interphase than in metaphase. For comparison the centromere size was more condensed in metaphase than in interphase. This implies a different folding behaviour for specific chromatin domains with opposite condensation behaviour.
journal_name
J Struct Bioljournal_title
Journal of structural biologyauthors
Batram C,Baddeley D,Kreth G,Cremer Cdoi
10.1016/j.jsb.2008.09.002subject
Has Abstractpub_date
2008-12-01 00:00:00pages
293-303issue
3eissn
1047-8477issn
1095-8657pii
S1047-8477(08)00223-2journal_volume
164pub_type
杂志文章abstract::Gap junction proteins, termed connexins, constitute a multigene family of polytopic membrane channel proteins that have four hydrophobic transmembrane domains with the N- and C-termini located on the cytoplasmic membrane face. The principal gap junction protein in the heart, alpha 1 connexin (also designated Cx43), me...
journal_title:Journal of structural biology
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journal_title:Journal of structural biology
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journal_title:Journal of structural biology
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journal_title:Journal of structural biology
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journal_title:Journal of structural biology
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journal_title:Journal of structural biology
pub_type: 杂志文章
doi:10.1006/jsbi.2000.4294
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abstract::The recent high-resolution structure of the toxin FraC derived from the sea anemone Actinia fragacea has provided new insight into the mechanism of pore formation by actinoporins. In this work, we report two new crystal forms of FraC in its oligomeric prepore conformation. Together with the previously reported structu...
journal_title:Journal of structural biology
pub_type: 杂志文章
doi:10.1016/j.jsb.2012.06.003
更新日期:2012-11-01 00:00:00
abstract::This article has been withdrawn at the request of the author(s) and/or editor. The Publisher apologizes for any inconvenience this may cause. The full Elsevier Policy on Article Withdrawal can be found at http://www.elsevier.com/locate/withdrawalpolicy. ...
journal_title:Journal of structural biology
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journal_title:Journal of structural biology
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journal_title:Journal of structural biology
pub_type: 杂志文章
doi:10.1006/jsbi.1995.1026
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journal_title:Journal of structural biology
pub_type: 杂志文章
doi:10.1016/j.jsb.2006.08.021
更新日期:2007-05-01 00:00:00
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journal_title:Journal of structural biology
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journal_title:Journal of structural biology
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abstract::OxlT is a bacterial transporter protein with 12 transmembrane segments that belongs to the Major Facilitator Superfamily of transporters. It facilitates the exchange of oxalate and formate across the membrane of the Gram-negative bacterium Oxalobacter formigenes. From an electron crystallographic analysis of two-dimen...
journal_title:Journal of structural biology
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abstract::Cryo-electron tomography (cryoET) allows 3D structural information to be obtained from cells and other biological samples in their close-to-native state. In combination with subtomogram averaging, detailed structures of repeating features can be resolved. CryoET data is collected as a series of images of the sample fr...
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journal_title:Journal of structural biology
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