Human CENP-A contains a histone H3 related histone fold domain that is required for targeting to the centromere.

Sullivan, Kevin F.; Hechenberger, Mirko; Masri, Khaled

doi:10.1083/jcb.127.3.581

Cited by 427 publications

(302 citation statements)

References 55 publications

(61 reference statements)

Supporting

Mentioning

295

Contrasting

Unclassified

Order By: Relevance

“…These results are entirely consistent with basic concepts concerning autoantibodies in systemic autoimmune diseases [15]. Among the three antigens, the cDNA encoding CENP-A was last cloned [16] but a detailed mapping of CENP-A has not been published to date. In a previous study [17], we identified one antigenic epitope of CENP-A at the N-terminal charged region (amino acid sequence 3±17) using ELISA with a synthetic peptide.…”

Section: Introductionsupporting

confidence: 87%

“…It might be due to the usage of the baculovirus system, which can induce modifications in the protein [23,29]. In the N-terminal part of CENP-A, four copies of the peptide Ser/Thr-Pro, which are good candidates for phosphorylation, are present [16]. Some ACA for CENP-A might show a striking preference for conformational epitopes by protein modifications such as phosphorylation.…”

Section: Discussionmentioning

confidence: 99%

“…The published sequence of CENP-A [16] was used to construct two kinds of synthetic peptides. Peptide A, PRRRSRKPEAPR-RRS, and peptide B, GPSRRGPSLGASSH, corresponding to residues 3±17 and residues 25±38, respectively, were synthesized with a C-terminal cysteine amide residue using a solid-phase method [20].…”

Section: Synthetic Peptidesmentioning

confidence: 99%

See 2 more Smart Citations

Autoepitopes on autoantigen centromere protein-A (CENP-A) are restricted to the N-terminal region, which has no homology with histone H3

Muro

Azuma²,

Onouchi³

et al. 2000

Clinical and Experimental Immunology

View full text Add to dashboard Cite

SUMMARYAnti-centromere autoantibodies (ACA) are commonly found in the serum of patients with a limited type of scleroderma and other systemic autoimmune diseases. CENP-A is one of the major antigens against ACA and a histone H3-like protein. To analyse the autoantigenic epitopes of CENP-A, a series of truncated peptides of human CENP-A were expressed in Escherichia coli and immunoblotting analysis was performed with 91 ACA 1 sera. Eighty sera (88%) with the ACA reacted to the 52-amino acids N-terminal region which is not homologous to H3, while no sera reacted to the C-terminus which has a sequence similarity with H3. Moreover, ELISA was also employed in this study using two synthetic peptides corresponding to the amino acid sequences 3±17 (peptide A) and 25±38 (peptide B). Peptides A and B were reactive to 78 (86%) and 79 (87%) of ACA, respectively. Core antigens of hepatitis B virus (HBV) and hepatitis C virus (HCV) have similar sequences to peptide A and/or peptide B, but three sera containing HBV without ACA and five sera containing HCV without ACA were found to be reactive to neither peptide. Centromere localization of CENP-A is dependent on the H3-like C-terminal domain which is not autoantigenic, while the antigenic N-terminal domain, which might play unidentified functional roles, should be an important region for the induction of ACA.

show abstract

Section: Introductionsupporting

confidence: 87%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Autoepitopes on autoantigen centromere protein-A (CENP-A) are restricted to the N-terminal region, which has no homology with histone H3

Muro

Azuma²,

Onouchi³

et al. 2000

Clinical and Experimental Immunology

View full text Add to dashboard Cite

show abstract

“…In this unit, we explain in detail how to perform a typical SNAP pulse labeling experiment in human cells. As an example, we will use HeLa cells that stably express a SNAP-tagged version of CENP-A, a centromere specific histone variant (Sullivan et al, 1994;Jansen et al, 2007). Using these CENP-A-SNAP cells, we have been able to show previously that the rate of centromeric CENP-A turnover corresponds to the rate of cell division, and thus that CENP-A turns over exclusively by dilution during DNA replication (Jansen et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

Analysis of Protein Turnover by Quantitative SNAP‐Based Pulse‐Chase Imaging

et al. 2012

View full text Add to dashboard Cite

Assessment of protein dynamics in living cells is crucial for understanding their biological properties and functions. The SNAP‐tag, a self labeling suicide enzyme, presents a tool with unique features that can be adopted for determining protein dynamics in living cells. Here we present detailed protocols for the use of SNAP in fluorescent pulse‐chase and quench‐chase‐pulse experiments. These time‐slicing methods provide powerful tools to assay and quantify the fate and turnover rate of proteins of different ages. We cover advantages and pitfalls of SNAP‐tagging in fixed‐ and live‐cell studies and evaluate the recently developed fast‐acting SNAPf variant. In addition, to facilitate the analysis of protein turnover datasets, we present an automated algorithm for spot recognition and quantification. Curr. Protoc. Cell Biol. 55:8.8.1‐8.8.34. © 2012 by John Wiley & Sons, Inc.

show abstract

“…In vivo, CenH3 homotypic nucleosomes associate with centromeric DNA in place of the typical H3s associated with the rest of the genome. The conserved HFD of CenH3 likely performs structural functions similar to the HFDs of other H3s (4) and also is required for targeting CENP-A to the centromere in mammalian cells (37). The precise functions of the divergent N termini are unknown, although it has been suggested that they interact with other centromeric proteins and may play a role in evolutionary suppression of meiotic drive (38).…”

mentioning

confidence: 99%

Centromeric Histone H3 Is Essential for Vegetative Cell Division and for DNA Elimination during Conjugation in Tetrahymena thermophila

Cui

Gorovsky

2006

Molecular and Cellular Biology

View full text Add to dashboard Cite

The Tetrahymena thermophila CNA1 gene encodes the centromeric H3, Cna1p. Green fluorescent protein (GFP)-tagged Cna1p localizes in micronuclei in dots whose number and behavior during mitosis and conjugation are consistent with centromeres. During interphase, Cna1p-GFP localizes in peripheral dots, suggesting centromeres are associated with the nuclear envelope. Newly synthesized Cna1p-GFP enters micronuclei in mitosis and accumulates in the nucleoplasm. Its deposition at centromeres starts at early S phase and continues through most of S phase. CNA1 is required for vegetative cell growth. Knockdown of CNA1 genes in the somatic macronucleus results in micronuclear DNA loss and delayed chromosome segregation during mitosis. During conjugation, Cna1p-GFP disappears from the centromeres in the developing macronucleus, consistent with centromeric sequences being internal eliminated sequences. Surprisingly, zygotic CNA1 is required for efficient elimination of germ line-specific sequences during development of the new macronuclei but not for the RNA interference pathway, through which sequences are targeted for elimination. Zygotically expressed Cna1p localizes in the spherical structures in which the later stages of DNA elimination occur, and these structures cannot be formed in the absence of zygotic CNA1, suggesting that, in addition to functioning in centromeres, Cna1p may also play a role in organizing the formation of the DNA elimination structures.

show abstract

Human CENP-A contains a histone H3 related histone fold domain that is required for targeting to the centromere.

Cited by 427 publications

References 55 publications

Autoepitopes on autoantigen centromere protein-A (CENP-A) are restricted to the N-terminal region, which has no homology with histone H3

Autoepitopes on autoantigen centromere protein-A (CENP-A) are restricted to the N-terminal region, which has no homology with histone H3

Analysis of Protein Turnover by Quantitative SNAP‐Based Pulse‐Chase Imaging

Centromeric Histone H3 Is Essential for Vegetative Cell Division and for DNA Elimination during Conjugation in Tetrahymena thermophila

Contact Info

Product

Resources

About