کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1953001 | 1057243 | 2009 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Importance of non-conserved distal carboxyl terminal amino acids in two peptidases belonging to the M1 family: Thermoplasma acidophilum Tricorn interacting factor F2 and Escherichia coli Peptidase N
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کلمات کلیدی
ARMASAM1 familymetallopeptidaseLTA4HAmCRRF7-amino-4-methylcoumarin - 7-آمینو-4-متیل کومارینAmino acids - اسید آمینه یا آمینو اسیدC-terminal domain - دامنه C ترمینالthermal denaturation temperature - دمای دگرگونی گرماییcircular dichroism - رنگ تابی دورانیANS - سالaccessible surface area - سطح دسترسی قابل دسترسRibosome recycling factor - عامل بازیافت ریبوزومleukotriene A4 hydrolase - لئوتریژن A4 هیدرولازwild type - نوع وحشی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Importance of non-conserved distal carboxyl terminal amino acids in two peptidases belonging to the M1 family: Thermoplasma acidophilum Tricorn interacting factor F2 and Escherichia coli Peptidase N Importance of non-conserved distal carboxyl terminal amino acids in two peptidases belonging to the M1 family: Thermoplasma acidophilum Tricorn interacting factor F2 and Escherichia coli Peptidase N](/preview/png/1953001.png)
چکیده انگلیسی
Enzymes belonging to the M1 family play important cellular roles and the key amino acids (aa) in the catalytic domain are conserved. However, C-terminal domain aa are highly variable and demonstrate distinct differences in organization. To address a functional role for the C-terminal domain, progressive deletions were generated in Tricorn interacting factor F2 from Thermoplasma acidophilum (F2) and Peptidase N from Escherichia coli (PepN). Catalytic activity was partially reduced in PepN lacking 4Â C-terminal residues (PepNÎC4) whereas it was greatly reduced in F2 lacking 10Â C-terminal residues (F2ÎC10) or PepN lacking eleven C-terminal residues (PepNÎC11). Notably, expression of PepNÎC4, but not PepNÎC11, in E. coliÎpepN increased its ability to resist nutritional and high temperature stress, demonstrating physiological significance. Purified C-terminal deleted proteins demonstrated greater sensitivity to trypsin and bound stronger to 8-amino 1-napthalene sulphonic acid (ANS), revealing greater numbers of surface exposed hydrophobic aa. Also, F2 or PepN containing large aa deletions in the C-termini, but not smaller deletions, were present in high amounts in the insoluble fraction of cell extracts probably due to reduced protein solubility. Modeling studies, using the crystal structure of E. coli PepN, demonstrated increase in hydrophobic surface area and change in accessibility of several aa from buried to exposed upon deletion of C-terminal aa. Together, these studies revealed that non-conserved distal C-terminal aa repress the surface exposure of apolar aa, enhance protein solubility, and catalytic activity in two soluble and distinct members of the M1 family.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimie - Volume 91, Issue 9, September 2009, Pages 1145-1155
Journal: Biochimie - Volume 91, Issue 9, September 2009, Pages 1145-1155
نویسندگان
Anujith Kumar, Manoj Bhosale, Surendranath Reddy, Narayanaswamy Srinivasan, Dipankar Nandi,