Abstract
Telomere-binding proteins play a crucial role in maintaining the stability of telomere structures. In this study, we found that GbTRB1, a double-stranded telomere-binding protein, can bind telomeric DNA., plays a pivotal role in telomere complex stability in Ginkgo biloba. The Myb domain in GbTRB1 is a key domain for binding to the telomeric dsDNA sequences, while the H1/H5 histone domain is a key domain for binding to the telomeric ssDNA sequences. We the first time reported that GbTRB1 can bind telomeric DNA. GbTRB1 interacts with GbTERT, the telomerase subunit, in vivo and in vitro. The telomere length was increased in GbTRB1-overexpressed transgenic Arabidopsis, suggesting GbTRB1 plays an important role in maintaining telomere stability and telomere length. Our results showed GbTRB1 can bind telomeric DNA. and interact with telomerase. This unusual dual role of GbTRB1 may partly explain the longevity mechanisms observed in Ginkgo biloba. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s12870-025-06668-7.