You are here

Prof. Abdussalam Azem

ביוכימיה וביולוגיה מולקו סגל אקדמי בכיר
Prof. Abdussalam Azem
Phone: 03-6409007
Another phone: 03-6405100
Fax: 03-6406834
Office: Sherman - Life Sciences, 629

Reseach Interests

Protein transport and folding:   Proteins are formed as long chains of amino acids that fold into very specific three-dimensional conformations, which are essential for their activity. In the crowded cellular environment, proteins are assisted by chaperone proteins to fold into their final, functional conformation [1, 2]. Nascent proteins take advantage of chaperone proteins to reach their functional structure, as do stress-denatured proteins. Additionally, most proteins that are transported across biological membranes traverse the membrane in an unfolded conformation [3-8]. The processes of unfolding for transport and refolding on the other side of the membrane both make use of chaperone proteins. Our laboratory focuses on two types of protein systems: the 60 kDa protein-folding system and the mitochondrial inner-membrane protein import system.


Protein folding by Cpn60:  The 60 kDa family of chaperone proteins, also known as "chaperonins", is composed of two types. We are studying type I chaperonins, tetradecameric oligomeric proteins composed of 60 kDa subunits (cpn60) that work together with small heptameric ring-shaped helper proteins composed of 10 kDa (cpn10) subunits [9, 10]. This system is over-expressed in response to heat-shock, prevents protein aggregation and helps stress-denatured proteins refold. Thus, the proteins are also called the 60 and 10 kDa heat-shock proteins (hsp's). Due to their tremendous stability, the best studied of these proteins are the GroEL (60 kDa subunits) and GroES (10 kDa subunits) of E. coli. Homologous proteins have been identified in mammalian, yeast and plant mitochondria as well as in plant chloroplasts [11, 12]. In our laboratory, we are studying the structure and function of mammalian mitochondrial and plant chloroplast chaperonins, both of which exhibit different structural characteristics than GroEL.


For a more detailed research description


Recent Publications

For a full list of publications


Since 2010  

Schusdziarra, C., Blamowska, M., Azem, A. and Hell, K. (in press) Methylation-controlled J-protein MCJ acts in the import of proteins into human mitochondria (in press). Human Molecular Genetics.


Vitlin Gruber, A., Nisemblat, S., Zizelski, G., Parnas, P., Dzikowski, R., Azem, A. and Weiss, W. (in press) P. falciparum cpn20 is a bona fide co-chaperonin that can replace GroES in E. coli. Plos ONE.


Parnas, A., Nisemblat, S., Weiss, C., Levy-Rimler, G., Pri-Or, A., Zor, T., Lund, P., Bross, P., Azem, A. (2012) Identification of Elements that Dictate the Specificity of Mitochondrial Hsp60 for its Co-chaperonin. Plos ONE. Plos ONE. 7 (12), e50318.


Kuo, W.Y., Huang, C.H., Liu, A.C.., Cheng, C.P., Li, S.H., Chang, W.C., Weiss, C., Azem, A., Jinn, T.L. (in press) Chaperonin 20 mediates iron superoxide dismutase (FeSOD) activity independent of its co-chaperonin role in Arabidopsis chloroplasts. New Phytol.


Iosefson, O., Sharon, S., Goloubinoff, P., Azem, A. (2012). Reactivation of protein aggregates by mortalin and Tid1-the human mitochondrial Hsp70 chaperone system. Cell Stress & Chaperones. 17, 57-66.


Marom, M., Azem, A. and Mokranjac, D. (2011) Understanding the molecular mechanism of protein translocation across the mitochondrial inner membrane: Still a long way to go. Biochem. Biophys. Acta (Biomembranes). 1808, 990-1001.


Marom, M.†, Dayan, D.†, Demishtein-Zohary, K., Mokranjac, D., Neupert, W. and Azem, A. (2011) Direct interaction of mitochondrial targeting presequences with purified components of the TIM23 complex. J. Biol. Chem. 286, 43809-15438.


Vitlin, A., Weiss, C., Demishtein-Zohary, K. Rasouly, A., Levin, D., Pisanty-Farchi, O., Breiman, A., Azem, A. (2011) Chloroplast β chaperonins from A. thaliana function with endogenous cpn10 homologs in vitro. Plant Mol. Biol. 77, 105-115.


Sharkia, R., Azem, A., Kaiya, Q., Zelnik, N. Mahajnah, M. (2010) Mental Retardation and Consanguinity in a Selected Region of the Israeli Arab Community. Cent. Eur. J. Med. 5, 91-96.


Iosefson, O. and Azem, A. (2010) Reconstitution of the mitochondrial Hsp70 (mortalin)-p53 interaction using purified proteins - Identification of additional interacting regions. FEBS Lett. 584, 1080-1084.


Azem, A., Tsfadia, Y., Hajouj, O., Shaked, I. and Daniel, E. (2010) Cross-linking with bifunctional reagents and its application to the study of the molecular symmetry and the arrangement of subunits in hexameric protein oligomers. Biochim. Biophys. Acta. 1804, 768-780.


Tel Aviv University, P.O. Box 39040, Tel Aviv 6997801, Israel
Developed by
Design by
Basch Interactive