Leucine as a signal molecule

Kostelac, Anja (2016) Leucine as a signal molecule. Bachelor's thesis, Faculty of Science > Department of Biology.

Language: Croatian

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Biosignalization helps cells to adapt to the extracellular conditions (environment) and indirectly communicate with environment by activating/silencing expression of target genes and metabolism, respectively. Signalization is based on conversion of extracellular signal to the intracellular signal which activates or inhibits many cellular processes. Transduction of the signal includes the process of signal amplification and signal translation from one type to another. After the signal has been interpreted, it provides a cell a specific information. One of the signal molecules is an amino acid L-leucine. The aim od this report was to present L-leucine as a signal molecule for gene transcription and metabolism. L-leucine is an signal that indicates nutrient-rich conditions and is transported into the cell by LAT1 transporter. Leucine-responsive regulatory protein, Lrp, and protein Sestrin2 are intracellular L-leucine sensors that are induced to conformational change by binding of leucine. Lrp, a Escherichia coli protein, is a transcriptional regulator which transduces L-leucine information to the DNA and therefore activates/represses transcription of target genes. In this way, L-leucine effects transcription of tRNA, rRNA, amino acid catabolism genes, fimbria and transcription factors genes. Sestrin2 is a mammalian cytosolic protein that transfers L-leucine signal through mediator proteins to the terminal signal acceptor – protein complex mTORC1. mTORC1 is an architecture that includes mTOR protein kinase. Once mTOR has phosphorilated protein, actvity of a protein is activated or repressed. Phosphorilated proteins take part in lipid and protein biosynthesis reactions, energy metabolism and autophagy. In this way, L-leucine acts on the metabolic pathways of the cell.

Item Type: Thesis (Bachelor's thesis)
Supervisor: Gruić Sovulj, Ita
Date: 2016
Number of Pages: 30
Subjects: NATURAL SCIENCES > Biology
Divisions: Faculty of Science > Department of Biology
Depositing User: Palma Dizdarevic
Date Deposited: 11 May 2017 12:29
Last Modified: 11 May 2017 12:29
URI: http://digre.pmf.unizg.hr/id/eprint/5527

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