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Term paper/ tubulin/ etc. : Lecture 6

6-1. Term paper/ tubulin/ etc. : Lecture 6. Term paper - getting started and finishing it: hints - tubulin folding pathway: complexity at its best. Term paper. You will have a better idea as to what you find interesting. Think of interesting questions that need to be addressed.

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Term paper/ tubulin/ etc. : Lecture 6

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  1. 6-1 Term paper/ tubulin/ etc.: Lecture 6 Term paper - getting started and finishing it: hints - tubulin folding pathway: complexity at its best

  2. Term paper You will have a better idea as to what you find interesting Think of interesting questions that need to be addressed Search and read the latest literature on that topic Write 5-page Term paper according to guidelines Pick out a topic that is broad (biogenesis, degradation or related topic) then narrow down a subject by reading a review or two (I will suggest some reviews) Narrow down subject even further, e.g., to a protein or a process 6-2 Patiently wait until the end of next week

  3. Tubulin assembly 6-3 α tubulin β tubulin αβ-heterodimer assembled microtubule http://cellbio.utmb.edu/cellbio/microtubule_structure.htm

  4. FtsZ crystal structure 6-4 - archaeal FtsZ is the homologue of eukaryotic tubulin - first tubulin to be crystallized; shows the power of crystallizing proteins from different sources - structure of alpha-beta-tubulin heterodimer is now also known (TREMENDOUSLY difficult to obtain; used electron diffraction) - same group also published structure of MreB, a bacterial protein that forms filaments and has a structure that resembles actin van den Ent et al. (2001) Prokaryotic origin of the actin cytoskeleton. Nature413, 39-44. Lowe and Amos (1998) Crystal structure of the bacterial cell-division protein FtsZ. Nature391, 203-6.

  5. 6-5 Tubulin folding pathway Tian et al. (1997) J. Cell Biol.138, 821-32.

  6. Crystal structure of Rbl2p, the cofactor A for b-tubulin folding 6-6 - Rbl2p is the yeast homologue of cofactor A - binds monomeric b-tubulin - suppresses deleterious effects of excess b-tubulin in vivo - competes with a-tubulin in the b-tubulin heterodimer (therefore binds near native state?) - surface mostly hydrophilic; dimer interface has hydrophobic residues - may act as a dimer

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