Journal of Cell Science & Therapy
Open Access

Structure-function properties of Kytococcus sedentarius WhiB1

9^th International Conference and Exhibition on Advanced Cell and Gene Therapy

March 21-22, 2019 | Rome, Italy

Meshari Alhadlaq

University of Sheffield, UK

Posters & Accepted Abstracts: J Cell Sci Ther

Abstract :

Kytococcus sedentarius (Ks) is an opportunistic bacterium involved in pitted keratolysis, cerebral cyst infections, endocarditis and bacteraemia. WhiB-like (Wbl) proteins are a family of proteins that are only located in actinomycetes and play important role in developmental processes. The C-terminal regions are rich in positively charged amino acids, suggesting a role in DNA-binding. The N-terminal regions possess four conserved cysteine residues that act as anchors for iron-sulfur clusters, which respond to redox stress. This study shows that: (i) the cluster can be isolated in three forms, (ii) the cluster is important to structure the protein and, (iii) the cluster is sensitive to spermine nitric oxide (NO) but not oxygen (O2). The significance is the iron-sulfur cluster of WhiB1 is a key factor in the protein function. The cluster modulates the conformation of the protein, changes the DNA-binding properties and allows the protein to respond to NO but not O2. These facts suggest that WhiB1 has a role as an NOresponsive gene regulator that could be important for survival and persistence in human macrophages.

Biography :

Meshari Alhadlaq has received his BS and MS in Molecular Biology from Qassim and Bangor Universities in Saudi Arabia and United Kingdom in 2007 and 2013 respectively. Then he joined the Molecular Biology and Biotechnology Department at the University of Sheffield as a PhD candidate in 2015, to study the structure and biochemistry of protein. Since then his studies focus on the characterisation and role of WhiB proteins of Kytococcus sedentarius.

E-mail: maalhadlaq1@sheffield.ac.uk