干旱区生态环境知识资源中心(Arid): Protection of zeta-crystallin by alpha-crystallin under thermal stress

Arid

DOI	10.1016/j.ijbiomac.2020.11.183
	Protection of zeta-crystallin by alpha-crystallin under thermal stress
	Malik, Ajamaluddin; Almaharfi, Hajar Ahmed; Khan, Javed Masood; Hisamuddin, Malik; Alamery, Salman Freeh; Haq, Samina Hyder; Ahmed, Mohammad Z.
通讯作者	Malik, A (corresponding author), King Saud Univ, Coll Sci, Dept Biochem, Bldg 5,Room 2A56,POB 2455, Riyadh 11451, Saudi Arabia.
来源期刊	INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
ISSN	0141-8130
EISSN	1879-0003
出版年	2021
卷号	167 页码:289-298
英文摘要	Cataract is one of the major causes of blindness worldwide. Several factors including post-translational modification, thermal and solar radiations promote cataractogenesis. The camel lens proteins survive very harsh desert conditions and resist cataractogenesis. The folding and aggregation mechanism of camel lens proteins are poorly characterized. The camel lens contains three ubiquitous crystallins (alpha-, beta-, and gamma-crystallin) and a novel protein (zeta-crystallin) in large amounts. In this study, a sequence similarity search of camel alpha-crystallin with that of other organisms showed that the camel alpha B-crystallin consists of an extended N-terminal domain. Our results indicate that camel alpha-crystallin efficiently prevented aggregation of zeta-crystallin, with or without an obligate cofactor up to 89 degrees C. It performed a quick and efficient holdase function irrespective of the unfolding stage or aggregation. Camel alpha-crystallin exhibits approximately 20% chaperone activity between 30 and 40 degrees C and is completely activated above 40 degrees C. Camel alpha-crystallin underwent a single reversible thermal transition without loss of beta-sheet secondary structure. Intrinsic tryptophan fluorescence and ANS binding experiments revealed two transitions which corresponded to activation of its chaperone function. In contrast to earlier studies, camel alpha-crystallin completely protected lens proteins during thermal stress. (C) 2020 Elsevier B.V. All rights reserved.
英文关键词	alpha-Crystallin zeta-Crystallin Cataract Dynamic multimode spectroscopy Chaperone
类型	Article
语种	英语
收录类别	SCI-E
WOS记录号	WOS:000606683200028
WOS关键词	CHAPERONE-LIKE ACTIVITY ; HEAT-SHOCK-PROTEIN ; B-CRYSTALLIN ; GUINEA-PIG ; QUATERNARY STRUCTURE ; A-CRYSTALLIN ; CAMELUS-DROMEDARIUS ; INDUCED AGGREGATION ; RISK-FACTOR ; HUMAN LENS
WOS类目	Biochemistry & Molecular Biology ; Chemistry, Applied ; Polymer Science
WOS研究方向	Biochemistry & Molecular Biology ; Chemistry ; Polymer Science
来源机构	King Saud University
资源类型	期刊论文
条目标识符	http://119.78.100.177/qdio/handle/2XILL650/347955
作者单位	[Malik, Ajamaluddin; Almaharfi, Hajar Ahmed; Alamery, Salman Freeh; Haq, Samina Hyder] King Saud Univ, Coll Sci, Dept Biochem, Bldg 5,Room 2A56,POB 2455, Riyadh 11451, Saudi Arabia; [Khan, Javed Masood] King Saud Univ, Fac Food & Agr Sci, Dept Food Sci & Nutr, Riyadh 11451, Saudi Arabia; [Hisamuddin, Malik] Jamia Millia Islamia, Ctr Interdisciplinary Res Basic Sci, New Delhi, India; [Ahmed, Mohammad Z.] King Saud Univ, Coll Pharm, Dept Pharmacognosy, Riyadh, Saudi Arabia
推荐引用方式 GB/T 7714	Malik, Ajamaluddin,Almaharfi, Hajar Ahmed,Khan, Javed Masood,et al. Protection of zeta-crystallin by alpha-crystallin under thermal stress[J]. King Saud University,2021,167:289-298.
APA	Malik, Ajamaluddin.,Almaharfi, Hajar Ahmed.,Khan, Javed Masood.,Hisamuddin, Malik.,Alamery, Salman Freeh.,...&Ahmed, Mohammad Z..(2021).Protection of zeta-crystallin by alpha-crystallin under thermal stress.INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES,167,289-298.
MLA	Malik, Ajamaluddin,et al."Protection of zeta-crystallin by alpha-crystallin under thermal stress".INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 167(2021):289-298.