Distribution of kinetochore (centromere) antigen in mammalian cell nuclei.

Möroi, Y; Hartman, A. L.; Nakane, Paul K.; Tan, Eng M.

doi:10.1083/jcb.90.1.254

Cited by 141 publications

(49 citation statements)

References 16 publications

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“…As shown in Fig. 5, the amino acid sequence for epitope I was also perfectly conserved in this species, suggesting that at least one of them might be the antigenic determinant commonto mammalian centromere proteins (4,13,16,17,20). In contrast, epitope II shared less homology, indicating that it would actually be the one that defines a human specificity.…”

Section: Resultsmentioning

confidence: 86%

“…Crossreactivity of affinityeluted anticentromere antibodies suggested that these three antigens shared someantigenic determinants, although the precise epitope of each antigen remains unknown(7). In addition, manyother mammaliancentromeres such as hamster, mouse (16,17), rat, muntjac, rat kangaroo (4), porcine, rabbit (13), and bovine (20) are also immunoreactive to the patient sera as well, suggesting the existence of another commonantigenic determi- Abbreviations: CENPs, centromere proteins; CENP-B, centromere protein B; IPTG, isopropyl-/3-D(-)-thiogalactopyranoside.…”

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confidence: 99%

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An Antigenic Determinant on Human Centromere Protein B (CENP-B) A vailable for Production of Human-Specific Anticentromere Antibodies in Mouse.

Sugimoto

Migita

Hagishita

et al. 1992

Cell Struct. Funct.

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Key words: Centromere protein B (CENP-B)/antigenic determinant/anticentromere antibodies/epitope mapping /mammalian cells ABSTRACT. Centromere protein B (CENP-B) is one of the centromere DNAbinding proteins constituting centromere heterochromatin throughout the cell cycles. Somecomponents of mammaliancentromeres including CENP-Bare target antigens for autoimmune disease patients, often those with scleroderma. Recent isolations of CENP-Bgenes from humanand mouse suggested that CENP-Bwas highly conserved among mammals. From the previous analysis of the reactivity of patient anticentromere sera, two autoepitopes have been located on the DNAbinding domain at the amino-terminal region. The amino acid sequences for both the epitopes are perfectly conserved in the two species, human and mouse. In this study, to identify a human-specific antigenic determinant, the remaining two epitopes were further located in separate carboxyl-terminal regions of humanCENP-B.Although the amino acid sequence of one epitope is identical to that of the corresponding region in mouse CENP-B,the other has a less homologous sequence. To confirm that the latter epitope was available for production of human-specific anticentromere antibodies, mice were immunizedwith the recombinant human CENP-Bproduct. One serum that exclusively stained human centromere structure, but not that of other mammals,was identified in the immunofluorescence microscopic observation. The epitope analysis showed that the less conserved one was recognized by this serum. These results suggested that the corresponding region defines the antigenic determinants for the species specificity.

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Section: Resultsmentioning

confidence: 86%

mentioning

confidence: 99%

An Antigenic Determinant on Human Centromere Protein B (CENP-B) A vailable for Production of Human-Specific Anticentromere Antibodies in Mouse.

Sugimoto

Migita

Hagishita

et al. 1992

Cell Struct. Funct.

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“…Antibodies to the paracentromeric regions, known to be constitutively heterochromatic, also delineate similarly large compact domains, and do not entail DNA denaturation (see, e.g., 43,51). The dimensions of these larger interphase domains approaches the 700 nm width of highly contracted metaphase chromosomes.…”

Section: Results and Discussion Dimensions Of Interphase And Metaphasmentioning

confidence: 99%

A unified model of eukaryotic chromosomes

1990

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A revised model of DNA packaging into chromosomes is presented. Its features are consistent with observed structural dimensions and the molecular periodicities related to transcription, replication and matrix attachment domains. Thetransitions between euchromatic, heterochromatic and metaphase states are explained simply. Molecular and physical properties of chromosomal bands, and their correlation with specific DNA sequence motifs are discussed.Key terms: Chromatin, chromosome structure, matrix, replication, Giemsa bands, repeated DNA The higher order molecular and physical structure of chromosomes is still poorly understood. The winding of the DNA double helix around histones to form 10 nm thick nucleosomes or "beads on a string," and the subsequent coiling of nucleosomes into solenoids of -30 nm x 10 nm is by now well-established. Each solenoid turn however encompasses only -1.2 kb of DNA, and is too small to embrace complex transcriptional and replication domains that may span several hundred kilobases of DNA. These larger "functional" units of DNA are likely to be arranged into hierarchical structures that can be recognized and conveniently utilized in a n orderly fashion. On a purely structural level, the delineation of metaphase chromosome bands by Giemsa staining suggests that such hierarchies exist; Giemsa bands encompass megabase (Mb) stretches of DNA and are not meaningless artifacts; for example, Giemsalight bands are preferentially digested by trypsin, indicating structural andior molecular components are specifically organized in these compartments, and overall binding patterns may be conserved in evolution (27). Furthermore, domains of similar large size, that may correspond to Giemsa bands, are involved in sister chromatid exchanges, translocations and replication. Sam Latt made many original contributions to the molecular organization of the genome, and one of his eminent contributions was the delineation of sister chromatid exchanges (32). In his honor, we present a physical model of chromosome structure that encompasses units of this size.We here build an updated model that incorporates the longer features of molecular gene organization that have become apparent in the last 10 years. Such features include units that range in size from very long linear lengths of DNA, as defined by chromosome banding techniques, pulse-field gel electrophoresis (PFGE), and high-resolution non-isotopic in-situ hybridization, through smaller DNA lengths of 30-120kb that periodically attach to matrix proteins and replication complexes. To date, no model of chromosome structure adequately addresses the folding or compaction of these longer DNA lengths in both interphase and metaphase chromosomes of known dimensions. Since these dimensional constraints are essential to any realistic model of chromosome folding, we first address the actual sizes of chromosome domains i n both interphase and metaphase chromosomes. The structure of interphase chromosomes is pivotal, since interphase cells carry out key functions such as...

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“…Thus, these changes may not be applicable to other chromosomes. In this regard, Moroi et al (22) previously examined the centromeres of acrocentric chromosomes located in the nucleoli. More relevant studies were recently completed in our laboratory.…”

Section: Formation Of Pericentromeres and Entire Chromatinmentioning

confidence: 99%

Differences in spatial localization and chromatin pattern during different phases of cell cycle between normal and cancer cells

et al. 1997

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We studied differences in chromatin patterns and the spatial localization of centromeres of chromosome 11 during the cell cycle between normal peripheral blood lymphocytes (PBL) and human promyclocytic leukemia cells (HL‐60) using fluorescence in situ hybridization. The pericentromeres in both cells were located at the periphery during Gq (quiescent) phase, but moved towards the nuclear center in G1 and mid‐S phase. During G2, the pericentromeres of PBL continued to move towards the nuclear center whereas those of HL‐60 returned to the periphery. The angle defining the spatial location of two pericentromeres, in reference to the center of the nucleus, increased in PBL cells from a mean of 67° during Gq phase to 106° during G1 phase (P < 0.01), and the two pericentromeres remained wide apart throughout the entire cell cycle. In HL‐60, the angle also increased during G1, but then decreased during mid‐S and G2 phases. Both cells exhibited pericentromeric signals during Gq that were round and compact, and the entire chromatin was loosely condensed. The signal became more loose and dispersed during the G1 and mid‐S phases. The pericentromere signal varied during G2 and was generally rod‐like or bipartite with condensation of the entire chromatin or chromosome‐like. Our results suggest that subtle but important differences in spatial localization of pericentromeres are present during the interphase between normal PBL and HL‐60 cells. Cytometry 27:327–335, 1997. © 1997 Wiley‐Liss, Inc.

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Distribution of kinetochore (centromere) antigen in mammalian cell nuclei.

Cited by 141 publications

References 16 publications

An Antigenic Determinant on Human Centromere Protein B (CENP-B) A vailable for Production of Human-Specific Anticentromere Antibodies in Mouse.

An Antigenic Determinant on Human Centromere Protein B (CENP-B) A vailable for Production of Human-Specific Anticentromere Antibodies in Mouse.

A unified model of eukaryotic chromosomes

Differences in spatial localization and chromatin pattern during different phases of cell cycle between normal and cancer cells

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