Bioinformatics study on the non-specific lipid transfer protein gene family in Camelina Sativa: focus on phosphorylation sites

سال انتشار: 1402
نوع سند: مقاله کنفرانسی
زبان: انگلیسی
مشاهده: 217

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شناسه ملی سند علمی:

AGRIHORMOZ01_032

تاریخ نمایه سازی: 20 شهریور 1402

چکیده مقاله:

Lipids are significant chemicals engaged in various aspects of growth and development in plants. Lipids and their derivatives involved in several important cell-signaling pathways. Non-specific lipid transfer proteins (nsLTPs) are small, basic proteins that are characterized by an eight-cysteine motif. The biological functions of nsLTPs proteins have been demonstrated to engage abiotic or biotic stress response. Phosphorylation as widespread proteins post-translational modification can change target site and activity of a protein. Camelina sativa has multiple agronomic attributes like resistance to insects and herbs and facile adaptation to every climatic condition. The main content of camelina seed is the oil. We performed a genome-wide analysis of the nsLTP gene family in Camelina sativa and identified ۱۰۴ nsLTP genes. Molecular weight (MW), isoelectric point (pI), aliphatic index, instability index and grand average of hydropathy (GRAVY) were predicted. The total number of amino acid of nsLTP proteins varied from ۹۰ to ۱۱۲۲ aa, CSnsLTP۱۰۳ was the smallest protein and CSnsLTP۴۷ was the largest protein. Molecular weight of nsLTP proteins varied between ۱۴.۵۴۵ to ۱۲۵۳۳۸.۱۲ kDa. The aliphatic index varied from ۶۲.۴۶ to۱۰۷.۴, and CSnsLTP۸۹ and CSnsLTP۲۴ had the highest and lowest aliphatic indices, respectively. The GRAVY values of Camelina Sativa were predicted between -۰.۵۸۴ to ۰.۷۳۲. The CSnsLTP۳۴, CSnsLTP۳۷ and CSnsLTP۶۵ had minimum (۵) and maximum (۴۳۵) number of phosphorylation sites, respectively. CSnsLTP۳۳ genes of Camelina Sativa have high number (۸۹) serine (serine-rich repeat) that could be changed by phosphorylation, and CSnsLTP۴۷ had high (۳۷) predicted phosphorylation sites on and Threonine CSnsLTP۴۷ had high (۷) predicted phosphorylation sites on Tyrosine. It can be concluded that acquired results provide further information about the nsLTP genes that will be helpful for functional analysis.

نویسندگان

Erfane Rastegar

Minab Higher Education Center, University of Hormozgan, Bandar Abbas, Iran.

Parviz Heidari

Faculty of Agriculture, Shahrood University of Technology, Shahrood, Iran.

Kimiya Beigi Dastgerdi

Minab Higher Education Center, University of Hormozgan, Bandar Abbas, Iran.

Mostafa Ahmadizadeh

Minab Higher Education Center, University of Hormozgan, Bandar Abbas, Iran.