结核分枝杆菌（Mycobacterium tuberculosis）的GroEL1蛋白是基因复制产物，作为热休克蛋白（HSP）一员，不但行使原有的助折叠分子伴侣功能，而且可作为抗原，在抗原呈递中起作用。另外，由于其独特的结构特点，GroEL1还具有多种生物功能，如作为蛋白分子伴侣，控制细胞因子依赖性肉芽肿的产生；作为DNA分子伴侣，保护DNA免受损害。而在分枝杆菌属的其他物种如耻垢分枝杆菌（Mycobacterium smegmatis）中却行使不同的生物学功能。这些功能产生的原因和机制有待进一步研究，从而为结核病的发生及结核杆菌的进化机制研究提供更多的依据。

Chaperonin GroEL1 in Mycobacterium tuberculosis is a product of gene duplication. As a member of heat shock proteins (HSPs), it not only promotes refolding of model substrates in vitro and in vivo, but also acts as an efficient antigen and performs function in antigen presentation. Besides, it has unique structure features, which possibly provide Mycobacterium tuberculosis with a variety series of biological functions such as regulating the cytokine-dependent granulomatous response in Mycobacterium tuberculosis infection as a protein-chaperonin, and associates with nucleoids to protect DNA as DNA-chaperonin. However, GroEL1 plays different roles in other species of Mycobacteria such as Mycobacterium smegmatis. The reasons and mechanisms of these functions need futher studies to be addressed, providing more basis for the research of the evolutionary mechanism of Mycobacterium tuberculosis.