CENPA Human

CENP-A was serendipitously discovered in 1985 by William Earnshaw during immunoblotting and immunostaining experiments using serum from CREST syndrome patients . This discovery highlighted the importance of CENP-A in centromere identity and function. The presence of CENP-A at centromeres is a defining feature that distinguishes centromeric chromatin from the rest of the chromosome.

CENP-A contains a histone fold domain, which allows it to replace histone H3 in centromeric nucleosomes . This replacement is critical for the assembly of the kinetochore, a protein complex that attaches chromosomes to the spindle fibers during mitosis and meiosis. The unique structure of CENP-A, particularly its N-terminal region, is essential for its function in centromere identity and propagation .

Recombinant CENP-A is produced using recombinant DNA technology, which involves inserting the CENPA gene into an expression system, such as bacteria or yeast, to produce the protein in large quantities. This recombinant protein is used in various research applications to study centromere function, chromosome segregation, and related cellular processes.

Research involving recombinant CENP-A has provided significant insights into the mechanisms of centromere identity and function. For example, studies have shown that CENP-A is an epigenetic marker for centromere identity, meaning that its presence at centromeres is inherited through cell divisions . Additionally, research has demonstrated that antibodies against CENP-A can interfere with oocyte meiosis, highlighting its importance in reproductive biology .

Antibodies against CENP-A are often found in patients with autoimmune diseases such as CREST syndrome, a form of systemic sclerosis . These antibodies can serve as important diagnostic markers for these conditions. Furthermore, understanding the role of CENP-A in centromere function can provide insights into chromosomal abnormalities and diseases related to chromosome missegregation.