Abdul Khalique PhD.
Dr. Abdul Khalique is a scientific advisor for Vgenomics based in the US. He is currently a research scientist at MD Anderson Cancer Center, previously he was a professor at National Institute of Health (NIH). He has over a decade of research experience including the field of rare diseases.
Dr. Khalique possesses expertise in RNA molecular biology techniques, tRNA Next-Gen Sequencing, and cell biology. With a focus on biotechnology, he earned his visiting fellowship from the National Institute of Health (NIH).
Dr. Khalique’s interest lies in the modification of transfer RNA (tRNA), which impacts mRNA decoding efficiency during translation. Recognizing the pivotal role of tRNA levels and modifications in gene regulation, he emphasizes the importance of accurate quantification to elucidate gene expression mechanisms. Overcoming the complexities of tRNA sequencing, Dr. Khalique has developed a cutting-edge Next-Generation sequencing method for tRNA library preparation, employing a specialized enzyme evolved from HIV-1 RT and Illumina Next-Seq500 sequencing.
Dr. Khalique brings 10+ years of scientific experience to Vgenomics.
Research articles
Dr. Khalique’s research revolves around tRNA expression and Transcriptome manipulation.
A versatile tRNA modification sensitive northern blot method with enhanced performance
The ~22 mitochondrial and ~45 cytosolic tRNAs contain several dozen different posttranscriptional modified nucleotides such that each carries a unique constellation that complements its function. Many tRNA modifications are linked to altered gene expression and their deficiencies due to mutations in tRNA modification enzymes (TMEs) are responsible for numerous diseases. Easily accessible methods to detect tRNA hypomodifications can facilitate progress in advancing such molecular studies. Our lab developed a northern blot method that can quantify relative levels of base modifications on multiple specific tRNAs ~10 years ago which has been used to characterize four different TME…
Translation of insulin granule proteins are regulated by PDI and PABP
Glucose mediated insulin biosynthesis is tightly regulated and shared between insulin granule proteins such as its processing enzymes, prohormone convertases, PC1/3 and PC2. However, the molecular players involved in the co-ordinated translation remain elusive. The trans-acting factors like PABP (Poly A Binding Protein) and PDI (Protein Disulphide Isomerize) binds to a conserved sequence in the 5’UTR of insulin mRNA and regulates its translation. Here, we demonstrate that 5’UTR of PC1/3 and PC2 also associate with PDI and PABP. We show that a’ and RRM 3-4 domains of PDI and PABP respectively, are necessary for RNA binding activity to the 5’UTRs of insulin and its processing enzymes.
Targeting mitochondrial and cytosolic substrates of TRIT1 isopentenyltransferase: Specificity determinants and tRNA-i6A37 profiles
The tRNA isopentenyltransferases (IPTases), which add an isopentenyl group to N6 of A37 (i6A37) of certain tRNAs, are among a minority of enzymes that modify cytosolic and mitochondrial tRNAs. Pathogenic mutations to the human IPTase, TRIT1, that decrease i6A37 levels, cause mitochondrial insufficiency that leads to neurodevelopmental disease. We show that TRIT1 encodes an amino-terminal mitochondrial targeting sequence (MTS) that directs mitochondrial import and modification of mitochondrial-tRNAs. Full understanding of IPTase function must consider the tRNAs selected for modification, which vary among species, and in their cytosol and mitochondria…
Interaction of HuDA and PABP at 5'UTR of mouse insulin2 regulates insulin biosynthesis
Understanding the regulation of insulin biosynthesis is important as it plays a central role in glucose metabolism. The mouse insulin gene2 (Ins2) has two splice variants; long (Ins2L) and short (Ins2S), that differ only in their 5’UTR sequence and Ins2S is the major transcript which translate more efficiently as compared to Ins2L. Here, we show that cellular factors bind preferentially to the Ins2L 5’UTR, and that PABP and HuD can bind to Ins2 splice variants and regulate its translation. In vitro binding assay with insulin 5’UTR and different HuD isoforms indicate that the ‘N’ terminal region of HuD is important for RNA binding and insulin translation repression…
Prolonged exposure to insulin with insufficient glucose leads to impaired Glut4 translocation
Insulin maintains glucose homeostasis by stimulating glucose uptake from extracellular environment to adipose and muscle tissue through glucose transporter (GLUT4). Insulin resistance plays a significant role in pathologies associated with type2 diabetes. It has been previously shown that hyperinsulinemia can lead to insulin resistance. In these studies very high levels of insulin was used to achieve insulin resistance. We hypothesized that one of the causes of type 2 diabetes could be insulin synthesis in the absence of glucose stimulation. We used CHO cell line, stably expressing Myc-GLUT4-GFP along with human insulin receptor to study the effect…
