التفاصيل البيبلوغرافية
| العنوان: |
The less conserved metal-binding site in human CRISP1 remains sensitive to zinc ions to permit protein oligomerization |
| المؤلفون: |
Sheng, Jie, Gadella, Bart M, Olrichs, Nick K, Kaloyanova, Dora V, Helms, J Bernd |
| المساهمون: |
LS Veterinaire biochemie, FAH klinische reproductie, Veterinaire biochemie, dB&C FR-RMSC FR, dES/dFAH FR, dB&C FR-RMSC RMSC |
| سنة النشر: |
2021 |
| مصطلحات موضوعية: |
General |
| الوصف: |
Cysteine-rich secretory proteins (CRISPs) are a subgroup of the CRISP, antigen 5 and PR-1 (CAP) superfamily that is characterized by the presence of a conserved CAP domain. Two conserved histidines in the CAP domain are proposed to function as a Zn2+-binding site with unknown function. Human CRISP1 is, however, one of the few family members that lack one of these characteristic histidine residues. The Zn2+-dependent oligomerization properties of human CRISP1 were investigated using a maltose-binding protein (MBP)-tagging approach in combination with low expression levels in XL-1 Blue bacteria. Moderate yields of soluble recombinant MBP-tagged human CRISP1 (MBP-CRISP1) and the MBP-tagged CAP domain of CRISP1 (MBP-CRISP1ΔC) were obtained. Zn2+ specifically induced oligomerization of both MBP-CRISP1 and MBP-CRISP1ΔC in vitro. The conserved His142 in the CAP domain was essential for this Zn2+ dependent oligomerization process, confirming a role of the CAP metal-binding site in the interaction with Zn2+. Furthermore, MBP-CRISP1 and MBP-CRISP1ΔC oligomers dissociated into monomers upon Zn2+ removal by EDTA. Condensation of proteins is characteristic for maturing sperm in the epididymis and this process was previously found to be Zn2+-dependent. The Zn2+-induced oligomerization of human recombinant CRISP1 may shed novel insights into the formation of functional protein complexes involved in mammalian fertilization. |
| نوع الوثيقة: |
article in journal/newspaper |
| وصف الملف: |
application/pdf |
| اللغة: |
English |
| تدمد: |
2045-2322 |
| Relation: |
https://dspace.library.uu.nl/handle/1874/411917 |
| الاتاحة: |
https://dspace.library.uu.nl/handle/1874/411917 |
| Rights: |
info:eu-repo/semantics/OpenAccess |
| رقم الانضمام: |
edsbas.343BBDDA |
| قاعدة البيانات: |
BASE |
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